Header list of 1tvi.pdb file
Complete list - r 2 2 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 29-JUN-04 1TVI TITLE SOLUTION STRUCTURE OF TM1509 FROM THERMOTOGA MARITIMA: VT1, A NESGC TITLE 2 TARGET PROTEIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: HYPOTHETICAL UPF0054 PROTEIN TM1509; 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: TM1509; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS ALPHA + BETA, MIXED 4-STRANDED BETA SHEET, FOUR HELIX BUNDLE, KEYWDS 2 STRUCTURAL GENOMICS, PROTEIN STRUCTURE INITIATIVE, NESGC, PSI, KEYWDS 3 NORTHEAST STRUCTURAL GENOMICS CONSORTIUM, UNKNOWN FUNCTION EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR C.H.PENHOAT,H.S.ATREYA,S.KIM,Z.LI,A.YEE,R.XIAO,D.MURRAY, AUTHOR 2 C.H.ARROWSMITH,T.SZYPERSKI,NORTHEAST STRUCTURAL GENOMICS CONSORTIUM AUTHOR 3 (NESG) REVDAT 6 02-MAR-22 1TVI 1 REMARK SEQADV REVDAT 5 09-JUN-09 1TVI 1 REVDAT REVDAT 4 24-FEB-09 1TVI 1 VERSN REVDAT 3 13-JAN-09 1TVI 1 JRNL REVDAT 2 25-JAN-05 1TVI 1 REMARK REVDAT 1 04-JAN-05 1TVI 0 JRNL AUTH C.H.PENHOAT,Z.LI,H.S.ATREYA,S.KIM,A.YEE,R.XIAO,D.MURRAY, JRNL AUTH 2 C.H.ARROWSMITH,T.SZYPERSKI JRNL TITL NMR SOLUTION STRUCTURE OF THERMOTOGA MARITIMA PROTEIN TM1509 JRNL TITL 2 REVEALS A ZN-METALLOPROTEASE-LIKE TERTIARY STRUCTURE. JRNL REF J.STRUCT.FUNCT.GENOM. V. 6 51 2005 JRNL REFN ISSN 1345-711X JRNL PMID 15965736 JRNL DOI 10.1007/S10969-005-5277-Z REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : DYANA 1.5, CYANA 1.05 REMARK 3 AUTHORS : GUNTERT, MUMENTHALER, WUTHRICH (DYANA), HERMANN, REMARK 3 GUNTERT, WUTHRICH (CYANA) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1TVI COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-JUL-04. REMARK 100 THE DEPOSITION ID IS D_1000022942. 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 : 1.0 ATMOSPHERE ATM REMARK 210 SAMPLE CONTENTS : 1 MM TM1509 (100% 15N, 100% REMARK 210 13C), 450 MM NACL, 25 MM NAHPO4, REMARK 210 10MM DTT, 0.01% NAN3, 1MM REMARK 210 BENZAMIDINE, 1 X INHIBITOR REMARK 210 COCKTAIL PILL, 95% H2O, 5% D2O; REMARK 210 1.2 MM TM1509 (100% 15N, 5% 13C), REMARK 210 450 MM NACL, 25 MM NAHPO4, 10MM REMARK 210 DTT, 0.01% NAN3, 1MM BENZAMIDINE, REMARK 210 1 X INHIBITOR COCKTAIL PILL, 95% REMARK 210 H2O, 5% D2O; 1.2 MM TM1509 (100% REMARK 210 15N, 5% 13C), 450 MM NACL, 25 REMARK 210 MM NAHPO4, 10MM DTT, 0.01% NAN3, REMARK 210 1MM BENZAMIDINE, 1 X INHIBITOR REMARK 210 COCKTAIL PILL, 95% H2O/5% D20 REMARK 210 WAS TITRATED WITH D20 TO REVEAL REMARK 210 SLOWLY EXCHANGING AMIDE PROTONS REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N REMARK 210 -SEPARATED_NOESY; GNHSQC; 3D REMARK 210 HNCO, 3D HNCACB, 3D HABCAB(CO)NH, REMARK 210 3D HNCAHA, 3D HCCHCOSY (C13,1H, REMARK 210 1H), 3D HCCHTOCSY (13C,13C,1H); REMARK 210 CT GCHSQC 2D SPECTRA 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 : MOLMOL 1.0, XEASY 1.3.3, TALOS REMARK 210 98.040.21.02 REMARK 210 METHOD USED : DYANA 1.5 WITH 30,000 TAD STEPS REMARK 210 AND SIMULATED ANNEALING 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: BOTH ALIPHATIC AND AROMATIC 3D_13C-SEPARATED_NOESY WERE REMARK 210 CONDUCTED 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 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 MODELS 1-20 REMARK 465 RES C SSSEQI REMARK 465 MET A -21 REMARK 465 GLY A -20 REMARK 465 THR A -19 REMARK 465 SER A -18 REMARK 465 HIS A -17 REMARK 465 HIS A -16 REMARK 465 HIS A -15 REMARK 465 HIS A -14 REMARK 465 HIS A -13 REMARK 465 HIS A -12 REMARK 465 SER A -11 REMARK 465 SER A -10 REMARK 465 GLY A -9 REMARK 465 ARG A -8 REMARK 465 GLU A -7 REMARK 465 ASN A -6 REMARK 465 LEU A -5 REMARK 465 TYR A -4 REMARK 465 PHE A -3 REMARK 465 GLN A -2 REMARK 465 GLY A -1 REMARK 465 HIS A 0 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 101 H LEU A 105 1.49 REMARK 500 O TYR A 129 H VAL A 133 1.50 REMARK 500 O TRP A 137 H ASN A 140 1.52 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 LYS A 9 104.83 -40.09 REMARK 500 1 ILE A 29 -58.36 -148.93 REMARK 500 1 ASP A 31 56.09 -166.22 REMARK 500 1 SER A 40 -165.26 -72.11 REMARK 500 1 PHE A 51 -51.98 -129.76 REMARK 500 1 ARG A 56 133.19 -174.11 REMARK 500 1 LEU A 65 130.85 -170.22 REMARK 500 1 ASP A 69 -76.53 -110.60 REMARK 500 1 VAL A 70 -60.78 -174.85 REMARK 500 1 ASN A 89 37.68 38.38 REMARK 500 1 TYR A 110 151.59 -36.27 REMARK 500 1 GLU A 113 -74.45 -142.79 REMARK 500 1 PHE A 114 41.05 39.30 REMARK 500 1 LYS A 117 -76.64 65.06 REMARK 500 1 SER A 142 -65.34 68.80 REMARK 500 1 ASP A 146 89.62 44.50 REMARK 500 2 LYS A 9 112.46 -39.82 REMARK 500 2 ILE A 29 99.26 -174.19 REMARK 500 2 ASP A 31 53.98 -164.98 REMARK 500 2 PHE A 51 -53.95 -127.36 REMARK 500 2 ARG A 56 132.92 -174.97 REMARK 500 2 LEU A 65 35.46 -168.90 REMARK 500 2 MET A 66 81.49 -56.89 REMARK 500 2 ASP A 69 111.36 169.15 REMARK 500 2 TYR A 71 60.63 -67.73 REMARK 500 2 ASN A 89 29.22 45.69 REMARK 500 2 TYR A 110 148.13 -37.05 REMARK 500 2 HIS A 112 68.58 -152.65 REMARK 500 2 GLU A 113 138.84 64.81 REMARK 500 2 PHE A 114 34.67 -141.67 REMARK 500 2 GLU A 115 83.67 81.77 REMARK 500 2 LYS A 117 90.35 -55.50 REMARK 500 2 ASN A 118 164.98 65.98 REMARK 500 2 SER A 119 120.52 163.04 REMARK 500 2 SER A 142 -60.24 69.84 REMARK 500 2 SER A 145 148.56 179.13 REMARK 500 2 LYS A 149 175.42 53.26 REMARK 500 3 LYS A 9 107.62 -40.24 REMARK 500 3 ASP A 31 97.65 -68.26 REMARK 500 3 SER A 40 -164.91 -78.34 REMARK 500 3 PHE A 51 -54.58 -130.55 REMARK 500 3 ARG A 56 128.34 -174.58 REMARK 500 3 LEU A 65 114.63 -170.39 REMARK 500 3 ASP A 69 -73.27 -127.90 REMARK 500 3 VAL A 70 -55.63 -168.78 REMARK 500 3 TYR A 71 29.84 38.23 REMARK 500 3 ASN A 89 29.92 39.86 REMARK 500 3 TYR A 110 139.17 67.73 REMARK 500 3 ASP A 111 71.70 -157.56 REMARK 500 3 HIS A 112 -63.49 -175.22 REMARK 500 REMARK 500 THIS ENTRY HAS 414 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: VT1 RELATED DB: TARGETDB DBREF 1TVI A 1 150 UNP Q9X1J7 Y1509_THEMA 1 150 SEQADV 1TVI MET A -21 UNP Q9X1J7 EXPRESSION TAG SEQADV 1TVI GLY A -20 UNP Q9X1J7 EXPRESSION TAG SEQADV 1TVI THR A -19 UNP Q9X1J7 EXPRESSION TAG SEQADV 1TVI SER A -18 UNP Q9X1J7 EXPRESSION TAG SEQADV 1TVI HIS A -17 UNP Q9X1J7 EXPRESSION TAG SEQADV 1TVI HIS A -16 UNP Q9X1J7 EXPRESSION TAG SEQADV 1TVI HIS A -15 UNP Q9X1J7 EXPRESSION TAG SEQADV 1TVI HIS A -14 UNP Q9X1J7 EXPRESSION TAG SEQADV 1TVI HIS A -13 UNP Q9X1J7 EXPRESSION TAG SEQADV 1TVI HIS A -12 UNP Q9X1J7 EXPRESSION TAG SEQADV 1TVI SER A -11 UNP Q9X1J7 EXPRESSION TAG SEQADV 1TVI SER A -10 UNP Q9X1J7 EXPRESSION TAG SEQADV 1TVI GLY A -9 UNP Q9X1J7 EXPRESSION TAG SEQADV 1TVI ARG A -8 UNP Q9X1J7 EXPRESSION TAG SEQADV 1TVI GLU A -7 UNP Q9X1J7 EXPRESSION TAG SEQADV 1TVI ASN A -6 UNP Q9X1J7 EXPRESSION TAG SEQADV 1TVI LEU A -5 UNP Q9X1J7 EXPRESSION TAG SEQADV 1TVI TYR A -4 UNP Q9X1J7 EXPRESSION TAG SEQADV 1TVI PHE A -3 UNP Q9X1J7 EXPRESSION TAG SEQADV 1TVI GLN A -2 UNP Q9X1J7 EXPRESSION TAG SEQADV 1TVI GLY A -1 UNP Q9X1J7 EXPRESSION TAG SEQADV 1TVI HIS A 0 UNP Q9X1J7 EXPRESSION TAG SEQRES 1 A 172 MET GLY THR SER HIS HIS HIS HIS HIS HIS SER SER GLY SEQRES 2 A 172 ARG GLU ASN LEU TYR PHE GLN GLY HIS MET ILE ARG ILE SEQRES 3 A 172 LEU GLY GLU GLY LYS GLY SER LYS LEU LEU GLU ASN LEU SEQRES 4 A 172 LYS GLU LYS LEU GLU GLU ILE VAL LYS LYS GLU ILE GLY SEQRES 5 A 172 ASP VAL HIS VAL ASN VAL ILE LEU VAL SER GLU ASP GLU SEQRES 6 A 172 ILE LYS GLU LEU ASN GLN GLN PHE ARG GLY GLN ASP ARG SEQRES 7 A 172 PRO THR ASP VAL LEU THR PHE PRO LEU MET GLU GLU ASP SEQRES 8 A 172 VAL TYR GLY GLU ILE TYR VAL CYS PRO LEU ILE VAL GLU SEQRES 9 A 172 GLU ASN ALA ARG GLU PHE ASN ASN THR PHE GLU LYS GLU SEQRES 10 A 172 LEU LEU GLU VAL VAL ILE HIS GLY ILE LEU HIS LEU ALA SEQRES 11 A 172 GLY TYR ASP HIS GLU PHE GLU ASP LYS ASN SER LYS GLU SEQRES 12 A 172 MET PHE GLU LYS GLN LYS LYS TYR VAL GLU GLU VAL TRP SEQRES 13 A 172 GLY GLU TRP ARG SER ASN PRO SER GLU ASP SER ASP PRO SEQRES 14 A 172 GLY LYS ARG HELIX 1 1 GLY A 10 LEU A 17 1 8 HELIX 2 2 LEU A 17 ILE A 29 1 13 HELIX 3 3 SER A 40 GLN A 50 1 11 HELIX 4 4 CYS A 77 PHE A 88 1 12 HELIX 5 5 THR A 91 GLY A 109 1 19 HELIX 6 6 SER A 119 ARG A 138 1 20 SHEET 1 A 4 ARG A 3 GLY A 6 0 SHEET 2 A 4 ASN A 35 LEU A 38 1 O VAL A 36 N LEU A 5 SHEET 3 A 4 GLU A 73 VAL A 76 1 O ILE A 74 N ILE A 37 SHEET 4 A 4 VAL A 60 LEU A 61 -1 N LEU A 61 O TYR A 75 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