Header list of 1zts.pdb file
Complete list - r 2 2 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 27-MAY-05 1ZTS
TITLE SOLUTION STRUCTURE OF BACILLUS SUBTILIS PROTEIN YQBG: NORTHEAST
TITLE 2 STRUCTURAL GENOMICS CONSORTIUM TARGET SR215
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYPOTHETICAL PROTEIN YQBG;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;
SOURCE 3 ORGANISM_TAXID: 1423;
SOURCE 4 GENE: YQBG;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PMGK;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PSR215-21.3
KEYWDS ALPHA, GFT NMR, STRUCTURAL GENOMICS, PROTEIN STRUCTURE INITIATIVE,
KEYWDS 2 PSI, NESG, SR215, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM,
KEYWDS 3 CYANA2.0, UNKNOWN FUNCTION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR G.LIU,Y.SHEN,R.XIAO,T.ACTON,L.MA,A.JOACHIMIAK,G.T.MONTELIONE,
AUTHOR 2 T.SZYPERSKI,NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG)
REVDAT 4 02-MAR-22 1ZTS 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1ZTS 1 VERSN
REVDAT 2 21-NOV-06 1ZTS 1 JRNL
REVDAT 1 12-JUL-05 1ZTS 0
JRNL AUTH G.LIU,Y.SHEN,R.XIAO,T.ACTON,L.C.MA,A.JOACHIMIAK,
JRNL AUTH 2 G.T.MONTELIONE,T.SZYPERSKI
JRNL TITL NMR STRUCTURE OF PROTEIN YQBG FROM BACILLUS SUBTILIS REVEALS
JRNL TITL 2 A NOVEL ALPHA-HELICAL PROTEIN FOLD.
JRNL REF PROTEINS V. 62 288 2006
JRNL REFN ISSN 0887-3585
JRNL PMID 16281282
JRNL DOI 10.1002/PROT.20666
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CYANA 2.0
REMARK 3 AUTHORS : P.GUNTERT ET AL.
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1ZTS COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-JUN-05.
REMARK 100 THE DEPOSITION ID IS D_1000033108.
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 : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.94 MM, U-15N,13C; NMR BUFFER
REMARK 210 6.5, 5% D2O, 0.02% NAN3, 10MM
REMARK 210 DTT, 5MM CACL2, 100MM NACL, 20MM
REMARK 210 MES,PH 6.5; 95% H2O, 5% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : SIMULTANEOUS HETERONUCLEAR
REMARK 210 RESOLVED [1H,1H] NOESY; GFT (4,3)
REMARK 210 D HNNCABCB; GFT (4,3)D CABCB(CO)
REMARK 210 NHN; GFT (4,3)D HABCAB(CO)NHN;
REMARK 210 GFT (4,3)D HCCH
REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CYANA 2.0, XEASY 1.3.1.3,
REMARK 210 NMRPIPE 2.3, AUTOSTRUCTURE 2.0.0,
REMARK 210 CYANA 1.0.5
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS DISTANCE
REMARK 210 GEOMETRY
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: BY USING CYANA2.0
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 PRO A 22 -170.75 -69.75
REMARK 500 1 HIS A 43 145.88 -174.70
REMARK 500 1 ASP A 44 -169.81 -107.46
REMARK 500 1 TYR A 50 59.64 -169.98
REMARK 500 1 ILE A 51 71.03 -114.80
REMARK 500 1 PRO A 54 -169.22 -69.77
REMARK 500 1 SER A 76 26.54 -162.79
REMARK 500 1 TYR A 81 97.19 58.32
REMARK 500 1 THR A 83 -170.18 -60.07
REMARK 500 1 GLU A 84 171.91 -51.95
REMARK 500 1 SER A 90 -168.41 -179.88
REMARK 500 1 LEU A 99 104.35 -51.84
REMARK 500 1 LYS A 113 82.14 51.43
REMARK 500 1 PRO A 114 -174.20 -69.78
REMARK 500 1 ALA A 115 52.08 -119.21
REMARK 500 1 PRO A 117 -164.30 -69.83
REMARK 500 1 GLU A 133 -74.40 -175.09
REMARK 500 2 PRO A 22 -170.09 -69.77
REMARK 500 2 HIS A 43 146.41 -174.46
REMARK 500 2 TYR A 50 54.20 -157.24
REMARK 500 2 TYR A 81 168.98 61.17
REMARK 500 2 GLU A 84 -170.45 -61.12
REMARK 500 2 ASP A 88 -170.12 -61.41
REMARK 500 2 TYR A 91 72.83 -103.38
REMARK 500 2 LEU A 93 177.89 -56.26
REMARK 500 2 LEU A 99 94.92 -62.13
REMARK 500 2 LYS A 113 160.27 -49.78
REMARK 500 2 PRO A 114 -175.42 -69.82
REMARK 500 2 PRO A 117 -164.40 -69.80
REMARK 500 2 GLU A 120 -169.88 -78.13
REMARK 500 2 LEU A 132 -74.50 -53.34
REMARK 500 2 GLU A 133 -67.12 -145.82
REMARK 500 2 HIS A 135 44.90 -100.00
REMARK 500 2 HIS A 138 -47.97 -170.26
REMARK 500 3 LEU A 3 -36.00 175.55
REMARK 500 3 PRO A 22 -170.68 -69.73
REMARK 500 3 HIS A 43 139.30 -175.35
REMARK 500 3 TYR A 50 64.90 -174.46
REMARK 500 3 ILE A 51 72.18 -113.93
REMARK 500 3 LEU A 53 79.72 -159.98
REMARK 500 3 PRO A 54 -170.51 -69.74
REMARK 500 3 SER A 76 34.46 -179.52
REMARK 500 3 LYS A 85 33.90 -93.82
REMARK 500 3 ASP A 88 -168.89 -100.27
REMARK 500 3 TYR A 89 159.57 63.90
REMARK 500 3 SER A 90 176.91 -55.97
REMARK 500 3 TYR A 91 48.39 -155.58
REMARK 500 3 LYS A 113 81.91 51.38
REMARK 500 3 PRO A 114 -175.61 -69.70
REMARK 500 3 ALA A 115 55.73 -151.92
REMARK 500
REMARK 500 THIS ENTRY HAS 415 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: SR215 RELATED DB: TARGETDB
DBREF 1ZTS A 1 131 UNP P45923 YQBG_BACSU 1 131
SEQADV 1ZTS SER A 98 UNP P45923 PRO 98 SEE REMARK 999
SEQADV 1ZTS LEU A 132 UNP P45923 EXPRESSION TAG
SEQADV 1ZTS GLU A 133 UNP P45923 EXPRESSION TAG
SEQADV 1ZTS HIS A 134 UNP P45923 EXPRESSION TAG
SEQADV 1ZTS HIS A 135 UNP P45923 EXPRESSION TAG
SEQADV 1ZTS HIS A 136 UNP P45923 EXPRESSION TAG
SEQADV 1ZTS HIS A 137 UNP P45923 EXPRESSION TAG
SEQADV 1ZTS HIS A 138 UNP P45923 EXPRESSION TAG
SEQADV 1ZTS HIS A 139 UNP P45923 EXPRESSION TAG
SEQRES 1 A 139 MET LEU LEU ILE THR PRO ASP GLU LEU LYS SER TYR SER
SEQRES 2 A 139 VAL PHE GLU SER VAL LYS THR ARG PRO ASP GLU LEU LEU
SEQRES 3 A 139 LYS GLN ASP ILE LEU GLU ALA THR ALA ASP ILE ILE LEU
SEQRES 4 A 139 LYS VAL GLY HIS ASP PHE SER ASP ALA GLU TYR ILE PRO
SEQRES 5 A 139 LEU PRO GLU THR VAL ARG LEU ALA LEU LEU LYS LEU SER
SEQRES 6 A 139 GLN PHE TYR ALA LEU ILE ASN GLY ASP GLU SER ILE ILE
SEQRES 7 A 139 LYS GLY TYR THR THR GLU LYS ILE GLY ASP TYR SER TYR
SEQRES 8 A 139 THR LEU GLY ASP GLY SER SER LEU GLN LYS PRO ASP VAL
SEQRES 9 A 139 TYR ALA LEU ILE LYS ASP TYR VAL LYS PRO ALA ASP PRO
SEQRES 10 A 139 ASP LEU GLU GLY ILE GLU ALA LYS VAL ARG MET ARG SER
SEQRES 11 A 139 ILE LEU GLU HIS HIS HIS HIS HIS HIS
HELIX 1 1 THR A 5 SER A 13 1 9
HELIX 2 2 PHE A 15 ARG A 21 1 7
HELIX 3 3 PRO A 22 GLY A 42 1 21
HELIX 4 4 PRO A 54 ILE A 71 1 18
HELIX 5 5 VAL A 104 LYS A 109 1 6
HELIX 6 6 ASP A 110 VAL A 112 5 3
HELIX 7 7 ALA A 124 SER A 130 1 7
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