Header list of 1t6r.pdb file
Complete list - r 2 2 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 07-MAY-04 1T6R
TITLE SOLUTION STRUCTURE OF TM1442, A PUTATIVE ANTI SIGMA FACTOR ANTAGONIST
TITLE 2 IN PHOSPHORYLATED STATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE ANTI-SIGMA FACTOR ANTAGONIST TM1442;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOTOGA MARITIMA;
SOURCE 3 ORGANISM_TAXID: 2336;
SOURCE 4 GENE: TM1442;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PET 25B(+), T7 RNA POLYMERASE;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET25B(+)
KEYWDS PHOSPHORYLATION, SOLUTION STRUCTURE, STRUCTURAL GENOMICS, PSI,
KEYWDS 2 PROTEIN STRUCTURE INITIATIVE, JOINT CENTER FOR STRUCTURAL GENOMICS,
KEYWDS 3 JCSG, UNKNOWN FUNCTION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR T.ETEZADY-ESFARJANI,W.PLACZEK,T.HERRMANN,S.A.LESLEY,K.WUTHRICH,JOINT
AUTHOR 2 CENTER FOR STRUCTURAL GENOMICS (JCSG)
REVDAT 4 02-MAR-22 1T6R 1 REMARK SEQADV LINK
REVDAT 3 24-FEB-09 1T6R 1 VERSN
REVDAT 2 31-MAY-05 1T6R 1 KEYWDS AUTHOR REMARK
REVDAT 1 24-MAY-05 1T6R 0
JRNL AUTH T.ETEZADY-ESFARJANI,W.J.PLACZEK,T.HERRMANN,K.WUTHRICH
JRNL TITL SOLUTION STRUCTURES OF THE PUTATIVE ANTI-SIGMA-FACTOR
JRNL TITL 2 ANTAGONIST TM1442 FROM THERMOTOGA MARITIMA IN THE FREE AND
JRNL TITL 3 PHOSPHORYLATED STATES.
JRNL REF MAGN.RESON.CHEM. V.C NO S61 2006
JRNL REFN ISSN 0749-1581
JRNL PMID 16826544
JRNL DOI 10.1002/MRC.1831
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NULL
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1T6R COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-MAY-04.
REMARK 100 THE DEPOSITION ID IS D_1000022382.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 313; 313; 313
REMARK 210 PH : 7.0; 7.0; 7.0
REMARK 210 IONIC STRENGTH : 20 MM SODIUMPHOSPHATE; 20 MM
REMARK 210 SODIUMPHOSPHATE; 20 MM
REMARK 210 SODIUMPHOSPHATE
REMARK 210 PRESSURE : AMBIENT; AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 2MM TM1442, 90% H2O, 10% D2O;
REMARK 210 1.5MM 15N-TM1442, 90% H2O, 10%
REMARK 210 D2O; 1.5MM 15N,13C-TM1442, 90%
REMARK 210 H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; 3D_13C-
REMARK 210 SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 900 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 3.5, DYANA 6.0, XEASY
REMARK 210 1.0
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH ACCEPTABLE
REMARK 210 COVALENT GEOMETRY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: NULL
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
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 4 ARG A 36 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 5 ARG A 90 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 7 LEU A 94 CB - CA - C ANGL. DEV. = 11.5 DEGREES
REMARK 500 8 ARG A 18 NE - CZ - NH2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 9 LEU A 81 CB - CG - CD1 ANGL. DEV. = 11.1 DEGREES
REMARK 500 15 TYR A 56 CB - CG - CD2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 18 ARG A 36 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
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 ASP A 7 66.43 -113.41
REMARK 500 1 ASP A 24 -166.83 -119.19
REMARK 500 1 ASN A 27 -40.26 -133.07
REMARK 500 1 SER A 52 -5.87 -59.44
REMARK 500 1 SER A 55 -46.56 -142.61
REMARK 500 1 SER A 87 -77.05 -56.67
REMARK 500 1 LYS A 102 -161.86 47.16
REMARK 500 2 ASN A 3 -67.50 -147.74
REMARK 500 2 GLU A 10 -118.27 -127.72
REMARK 500 2 GLN A 11 -176.48 54.39
REMARK 500 2 ASP A 12 -99.24 33.95
REMARK 500 2 ASP A 13 -1.89 -146.16
REMARK 500 2 LYS A 102 -155.98 47.81
REMARK 500 3 GLU A 10 31.04 -141.98
REMARK 500 3 ASP A 12 -83.12 -113.84
REMARK 500 3 ASP A 13 -2.42 -161.28
REMARK 500 3 THR A 41 43.12 -144.94
REMARK 500 3 SER A 43 -22.61 60.35
REMARK 500 3 SER A 55 -51.02 -121.59
REMARK 500 3 HIS A 96 42.27 38.78
REMARK 500 3 ILE A 100 -67.73 -105.72
REMARK 500 3 LYS A 102 -167.53 51.76
REMARK 500 4 ASN A 3 -175.01 52.90
REMARK 500 4 GLN A 11 -87.21 -131.51
REMARK 500 4 ASP A 12 83.48 -69.28
REMARK 500 4 ASP A 13 -5.57 40.87
REMARK 500 4 ASP A 24 179.95 168.44
REMARK 500 4 ASN A 27 -32.57 -137.17
REMARK 500 4 LEU A 84 109.36 -53.58
REMARK 500 4 LYS A 85 96.93 -69.33
REMARK 500 4 GLU A 86 -79.44 23.97
REMARK 500 4 LYS A 102 -166.05 49.35
REMARK 500 5 ASN A 3 -82.15 62.82
REMARK 500 5 ASN A 27 -44.94 -138.24
REMARK 500 5 THR A 41 -60.51 -92.39
REMARK 500 5 SER A 55 -39.87 -141.92
REMARK 500 5 LEU A 81 -139.43 -89.40
REMARK 500 5 SER A 82 167.44 164.84
REMARK 500 5 SER A 83 61.37 61.34
REMARK 500 5 LYS A 102 -168.51 47.23
REMARK 500 5 VAL A 107 -39.08 -37.51
REMARK 500 6 ASP A 13 4.81 -68.87
REMARK 500 6 ARG A 18 95.05 -69.18
REMARK 500 6 ASP A 22 15.22 -144.14
REMARK 500 6 ILE A 23 70.99 40.74
REMARK 500 6 ASN A 27 -41.61 -143.67
REMARK 500 6 SER A 55 -40.19 -130.31
REMARK 500 6 TYR A 56 -78.86 -75.48
REMARK 500 6 MET A 57 125.32 52.91
REMARK 500 6 ILE A 100 -70.97 -111.13
REMARK 500
REMARK 500 THIS ENTRY HAS 176 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLN A 11 ASP A 12 7 147.10
REMARK 500 SER A 53 VAL A 54 12 149.65
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 1 ARG A 36 0.10 SIDE CHAIN
REMARK 500 2 ARG A 36 0.14 SIDE CHAIN
REMARK 500 5 ARG A 36 0.08 SIDE CHAIN
REMARK 500 5 TYR A 56 0.08 SIDE CHAIN
REMARK 500 7 TYR A 26 0.08 SIDE CHAIN
REMARK 500 8 ARG A 18 0.09 SIDE CHAIN
REMARK 500 8 ARG A 36 0.11 SIDE CHAIN
REMARK 500 9 TYR A 56 0.09 SIDE CHAIN
REMARK 500 9 PHE A 79 0.09 SIDE CHAIN
REMARK 500 11 ARG A 36 0.15 SIDE CHAIN
REMARK 500 12 ARG A 18 0.13 SIDE CHAIN
REMARK 500 12 ARG A 36 0.11 SIDE CHAIN
REMARK 500 15 ARG A 36 0.14 SIDE CHAIN
REMARK 500 15 ARG A 90 0.09 SIDE CHAIN
REMARK 500 16 ARG A 18 0.11 SIDE CHAIN
REMARK 500 16 PHE A 79 0.09 SIDE CHAIN
REMARK 500 17 TYR A 26 0.07 SIDE CHAIN
REMARK 500 18 ARG A 18 0.08 SIDE CHAIN
REMARK 500 20 ARG A 18 0.11 SIDE CHAIN
REMARK 500 20 TYR A 26 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 17 SEP A 59 -10.11
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1SBO RELATED DB: PDB
REMARK 900 SOLUTION STRUCUTRE OF TM1442, APUTATIVE ANTI SIGMA FACTOR ANTAGONIST
REMARK 900 RELATED ID: 283301 RELATED DB: TARGETDB
DBREF 1T6R A 1 110 UNP Q9X1F5 Y1442_THEMA 1 110
SEQADV 1T6R SEP A 59 UNP Q9X1F5 SER 59 MODIFIED RESIDUE
SEQRES 1 A 110 MET ASN ASN LEU LYS LEU ASP ILE VAL GLU GLN ASP ASP
SEQRES 2 A 110 LYS ALA ILE VAL ARG VAL GLN GLY ASP ILE ASP ALA TYR
SEQRES 3 A 110 ASN SER SER GLU LEU LYS GLU GLN LEU ARG ASN PHE ILE
SEQRES 4 A 110 SER THR THR SER LYS LYS LYS ILE VAL LEU ASP LEU SER
SEQRES 5 A 110 SER VAL SER TYR MET ASP SEP ALA GLY LEU GLY THR LEU
SEQRES 6 A 110 VAL VAL ILE LEU LYS ASP ALA LYS ILE ASN GLY LYS GLU
SEQRES 7 A 110 PHE ILE LEU SER SER LEU LYS GLU SER ILE SER ARG ILE
SEQRES 8 A 110 LEU LYS LEU THR HIS LEU ASP LYS ILE PHE LYS ILE THR
SEQRES 9 A 110 ASP THR VAL GLU GLU ALA
MODRES 1T6R SEP A 59 SER PHOSPHOSERINE
HET SEP A 59 15
HETNAM SEP PHOSPHOSERINE
HETSYN SEP PHOSPHONOSERINE
FORMUL 1 SEP C3 H8 N O6 P
HELIX 1 1 ASN A 27 THR A 42 1 16
HELIX 2 2 ASP A 58 ASN A 75 1 18
HELIX 3 3 LYS A 85 LEU A 94 1 10
HELIX 4 4 HIS A 96 PHE A 101 1 6
SHEET 1 A 4 LYS A 5 VAL A 9 0
SHEET 2 A 4 ALA A 15 GLN A 20 -1 O GLN A 20 N LYS A 5
SHEET 3 A 4 ILE A 47 ASP A 50 1 O VAL A 48 N ALA A 15
SHEET 4 A 4 ILE A 80 SER A 82 1 O SER A 82 N LEU A 49
LINK C ASP A 58 N SEP A 59 1555 1555 1.33
LINK C SEP A 59 N ALA A 60 1555 1555 1.34
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