Header list of 1sbo.pdb file
Complete list - r 2 2 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 10-FEB-04 1SBO TITLE SOLUTION STRUCTURE OF PUTATIVE ANTI SIGMA FACTOR ANTAGONIST FROM TITLE 2 THERMOTOGA MARITIMA (TM1442) 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: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET25B(+) KEYWDS OPEN SANDWICH, JCSG, STRUCTURAL GENOMICS, JOINT CENTER FOR STRUCTURAL KEYWDS 2 GENOMICS, PSI, PROTEIN STRUCTURE INITIATIVE, UNKNOWN FUNCTION EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR T.ETEZADY-ESFARJAINI,W.J.PLACZEK,T.HERRMANN,S.A.LESLEY,K.WUTHRICH, AUTHOR 2 JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG) REVDAT 3 02-MAR-22 1SBO 1 REMARK REVDAT 2 24-FEB-09 1SBO 1 VERSN REVDAT 1 21-DEC-04 1SBO 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 : XWINNMR 3.5, ATNOS/CANDID/DYANA 6.0 REMARK 3 AUTHORS : BRUKER GMBH (XWINNMR), GUNTERT, P., HERRMANN, T. REMARK 3 (ATNOS/CANDID/DYANA) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1SBO COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-FEB-04. REMARK 100 THE DEPOSITION ID IS D_1000021581. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 313 REMARK 210 PH : 4.8 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 2 MM TM1442 U-15N ; 20 MM SODIUM REMARK 210 ACETATE; 2.5 MM TM1442; 20 MM REMARK 210 SODIUM ACETATE; 2 MM TM1442 U- REMARK 210 15N, 13C; 20 MM SODIUM ACETATE REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 2D REMARK 210 NOESY; 3D_13C-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 : ATNOS/CANDID/DYANA 6.0 REMARK 210 METHOD USED : DISTANCE GEOMETRY REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST REMARK 210 ENERGY 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 LEU A 84 CB - CG - CD2 ANGL. DEV. = 10.7 DEGREES REMARK 500 12 TYR A 26 CB - CG - CD1 ANGL. DEV. = -4.0 DEGREES REMARK 500 13 ARG A 90 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES REMARK 500 14 ARG A 90 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES REMARK 500 14 ARG A 90 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES REMARK 500 17 LEU A 65 CB - CG - CD1 ANGL. DEV. = 11.3 DEGREES REMARK 500 17 ARG A 90 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES REMARK 500 19 LEU A 84 CB - CG - CD2 ANGL. DEV. = 10.5 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 ASN A 3 86.18 -158.97 REMARK 500 1 LEU A 4 130.78 55.35 REMARK 500 1 ILE A 8 112.75 56.54 REMARK 500 1 GLN A 11 -153.64 -87.07 REMARK 500 1 GLU A 30 -71.55 -57.70 REMARK 500 1 GLN A 34 0.20 -65.59 REMARK 500 1 LEU A 35 -52.25 -120.32 REMARK 500 1 HIS A 96 19.34 55.37 REMARK 500 1 PHE A 101 -158.09 -120.98 REMARK 500 2 LYS A 5 -179.17 164.57 REMARK 500 2 ILE A 8 127.52 64.35 REMARK 500 2 GLN A 11 -148.64 -80.04 REMARK 500 2 GLU A 30 -71.93 -63.63 REMARK 500 2 HIS A 96 32.34 76.10 REMARK 500 2 PHE A 101 -166.86 -118.11 REMARK 500 3 LYS A 5 -160.84 -160.00 REMARK 500 3 ILE A 8 123.30 60.06 REMARK 500 3 GLN A 11 -162.71 -103.87 REMARK 500 3 LYS A 70 -72.85 -90.13 REMARK 500 3 ASP A 105 -64.03 -91.31 REMARK 500 4 ASN A 3 88.52 -150.28 REMARK 500 4 ILE A 8 110.11 42.22 REMARK 500 4 GLN A 11 -151.40 -88.06 REMARK 500 4 ASP A 22 159.36 -47.80 REMARK 500 4 SER A 83 64.11 60.16 REMARK 500 4 HIS A 96 4.58 59.45 REMARK 500 5 ASN A 3 57.82 -175.54 REMARK 500 5 LEU A 4 126.91 62.67 REMARK 500 5 ILE A 8 116.52 62.26 REMARK 500 5 GLN A 11 -158.95 -79.71 REMARK 500 5 ASP A 22 -169.96 -69.81 REMARK 500 5 SER A 28 -2.10 -58.87 REMARK 500 5 SER A 59 2.62 -57.06 REMARK 500 5 LYS A 99 4.35 -62.14 REMARK 500 5 PHE A 101 -161.65 -126.32 REMARK 500 6 LYS A 5 -170.73 -172.00 REMARK 500 6 ILE A 8 129.63 57.67 REMARK 500 6 PHE A 101 -169.97 -118.19 REMARK 500 7 LEU A 4 130.08 65.28 REMARK 500 7 ILE A 8 106.65 41.23 REMARK 500 7 GLN A 11 -155.65 -80.04 REMARK 500 7 SER A 55 -20.09 -156.88 REMARK 500 7 PHE A 79 118.81 -167.91 REMARK 500 7 PHE A 101 -168.63 -124.54 REMARK 500 7 ASP A 105 -76.50 -101.78 REMARK 500 8 ASN A 3 38.98 -151.33 REMARK 500 8 LEU A 4 138.19 69.72 REMARK 500 8 LYS A 5 -175.51 -178.65 REMARK 500 8 ILE A 8 126.79 63.15 REMARK 500 8 GLN A 11 -153.95 -85.99 REMARK 500 REMARK 500 THIS ENTRY HAS 130 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 THR A 41 THR A 42 2 -136.03 REMARK 500 GLY A 21 ASP A 22 4 147.67 REMARK 500 THR A 41 THR A 42 4 -141.64 REMARK 500 THR A 41 THR A 42 6 -147.68 REMARK 500 THR A 41 THR A 42 7 -147.22 REMARK 500 MET A 1 ASN A 2 8 140.58 REMARK 500 THR A 41 THR A 42 10 -147.20 REMARK 500 THR A 41 THR A 42 13 -137.64 REMARK 500 THR A 41 THR A 42 14 -145.04 REMARK 500 SER A 53 VAL A 54 17 -148.06 REMARK 500 THR A 41 THR A 42 20 -147.44 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 90 0.11 SIDE CHAIN REMARK 500 4 ARG A 18 0.08 SIDE CHAIN REMARK 500 5 TYR A 26 0.08 SIDE CHAIN REMARK 500 10 ARG A 18 0.08 SIDE CHAIN REMARK 500 13 ARG A 90 0.09 SIDE CHAIN REMARK 500 16 TYR A 26 0.07 SIDE CHAIN REMARK 500 17 ARG A 36 0.13 SIDE CHAIN REMARK 500 17 ARG A 90 0.09 SIDE CHAIN REMARK 500 18 ARG A 90 0.10 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1AUZ RELATED DB: PDB REMARK 900 SOLUTION STRUCTURE OF SPOIIAA, A PHOSPHORYLATABLE COMPONENT OF THE REMARK 900 SYSTEM THAT REGULATES TRANSCRIPTION FACTOR -F OF BACILLUS SUBTILIS, REMARK 900 NMR, 24 STRUCTURES REMARK 900 RELATED ID: 283301 RELATED DB: TARGETDB DBREF 1SBO A 1 110 UNP Q9X1F5 Y1442_THEMA 1 110 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 SER 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 HELIX 1 1 SER A 29 ASN A 37 1 9 HELIX 2 2 ASN A 37 THR A 42 1 6 HELIX 3 3 ASP A 58 ASN A 75 1 18 HELIX 4 4 LYS A 85 THR A 95 1 11 HELIX 5 5 LEU A 97 PHE A 101 5 5 HELIX 6 6 THR A 106 ALA A 110 5 5 SHEET 1 A 3 LYS A 5 LEU A 6 0 SHEET 2 A 3 LYS A 14 GLN A 20 -1 O GLN A 20 N LYS A 5 SHEET 3 A 3 VAL A 9 GLU A 10 -1 N VAL A 9 O ILE A 16 SHEET 1 B 4 LYS A 5 LEU A 6 0 SHEET 2 B 4 LYS A 14 GLN A 20 -1 O GLN A 20 N LYS A 5 SHEET 3 B 4 LYS A 46 ASP A 50 1 O VAL A 48 N VAL A 17 SHEET 4 B 4 GLU A 78 SER A 82 1 O ILE A 80 N ILE A 47 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