Header list of 1te7.pdb file
Complete list - r 2 2 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 24-MAY-04 1TE7 TITLE SOLUTION NMR STRUCTURE OF PROTEIN YQFB FROM ESCHERICHIA COLI. TITLE 2 NORTHEAST STRUCTURAL GENOMICS CONSORTIUM TARGET ET99 COMPND MOL_ID: 1; COMPND 2 MOLECULE: HYPOTHETICAL UPF0267 PROTEIN YQFB; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI; SOURCE 3 ORGANISM_TAXID: 562; SOURCE 4 GENE: YQFB; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS ALPHA + BETA, STRUCTURAL GENOMICS, PSI, PROTEIN STRUCTURE INITIATIVE, KEYWDS 2 NORTHEAST STRUCTURAL GENOMICS CONSORTIUM, NESG, UNKNOWN FUNCTION EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR H.S.ATREYA,Y.SHEN,A.YEE,C.ARROWSMITH,T.SZYPERSKI,NORTHEAST STRUCTURAL AUTHOR 2 GENOMICS CONSORTIUM (NESG) REVDAT 4 02-MAR-22 1TE7 1 REMARK ATOM REVDAT 3 24-FEB-09 1TE7 1 VERSN REVDAT 2 05-JUL-05 1TE7 1 JRNL REVDAT 1 04-JAN-05 1TE7 0 JRNL AUTH Y.SHEN,H.S.ATREYA,G.LIU,T.SZYPERSKI JRNL TITL G-MATRIX FOURIER TRANSFORM NOESY-BASED PROTOCOL FOR JRNL TITL 2 HIGH-QUALITY PROTEIN STRUCTURE DETERMINATION JRNL REF J.AM.CHEM.SOC. V. 127 9085 2005 JRNL REFN ISSN 0002-7863 JRNL PMID 15969587 JRNL DOI 10.1021/JA0501870 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PROSA 6, DYANA 5 REMARK 3 AUTHORS : GUENTERT (PROSA), GUENTERT, P. (DYANA) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1TE7 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-JUN-04. REMARK 100 THE DEPOSITION ID IS D_1000022577. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : NULL REMARK 210 PH : 6.5 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : 1MM U-13C,15N YQFB,25 MM NA REMARK 210 PHOSPHATE, 400 MM NACL, 1 MM DTT, REMARK 210 20 MM ZNCL2, 0.01% NAN3, 90% REMARK 210 H2O, 10% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : GFT (4,3)D HNNCABCA; GFT (4,3)D REMARK 210 CABCA(CO)NHN; GFT (5,2)D HACACONHN; GFT (4,3)D HCCH COSY; 3D 15N, REMARK 210 13CALIPHATIC,13CAROMATIC-RESOLVED [1H,1H]-NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : INOVA REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : XEASY 1, AUTOASSIGN 1 REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS WITH REMARK 210 DYANA REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST REMARK 210 RESTRAINT VIOLATIONS,STRUCTURES REMARK 210 WITH THE LOWEST 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 H ARG A 26 O TYR A 96 1.46 REMARK 500 H LEU A 39 O ILE A 53 1.50 REMARK 500 O LEU A 63 H THR A 67 1.58 REMARK 500 O GLU A 72 H MET A 76 1.58 REMARK 500 O ASP A 27 H GLU A 30 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 PHE A 8 117.46 -162.19 REMARK 500 1 PHE A 9 155.97 -37.41 REMARK 500 1 ARG A 20 94.08 43.01 REMARK 500 1 SER A 31 104.05 -38.04 REMARK 500 1 HIS A 32 -138.20 -85.29 REMARK 500 1 PHE A 33 -167.35 -54.54 REMARK 500 1 ASP A 46 43.34 164.93 REMARK 500 1 ASP A 47 15.32 -141.05 REMARK 500 1 TYR A 49 65.69 37.93 REMARK 500 1 THR A 56 -41.72 -131.35 REMARK 500 1 THR A 62 -153.54 -70.04 REMARK 500 1 LEU A 63 -72.81 -100.54 REMARK 500 1 LEU A 66 -39.89 -170.51 REMARK 500 1 THR A 67 153.60 -42.00 REMARK 500 1 ASN A 75 -61.96 -147.34 REMARK 500 1 TYR A 89 150.83 162.33 REMARK 500 1 GLN A 92 53.34 -116.05 REMARK 500 1 GLN A 94 150.04 -37.68 REMARK 500 2 ASN A 4 170.11 -47.70 REMARK 500 2 PHE A 9 162.39 -42.44 REMARK 500 2 LYS A 21 101.44 -38.63 REMARK 500 2 HIS A 32 -135.11 -108.86 REMARK 500 2 PHE A 33 177.15 -47.88 REMARK 500 2 GLU A 45 -31.55 -39.11 REMARK 500 2 ASP A 46 -35.71 177.23 REMARK 500 2 ASP A 47 -21.26 164.75 REMARK 500 2 THR A 62 -153.80 -68.18 REMARK 500 2 LEU A 63 -71.87 -100.47 REMARK 500 2 ASP A 64 -9.47 -57.25 REMARK 500 2 LEU A 66 -40.79 -172.54 REMARK 500 2 THR A 67 153.23 -42.83 REMARK 500 2 ASN A 75 -59.37 -148.11 REMARK 500 2 TYR A 89 148.02 165.11 REMARK 500 2 GLN A 94 144.88 -34.71 REMARK 500 3 GLN A 2 81.33 179.78 REMARK 500 3 PHE A 9 163.99 -40.23 REMARK 500 3 ARG A 20 94.15 42.96 REMARK 500 3 LYS A 21 152.66 -37.94 REMARK 500 3 PHE A 33 -147.94 -176.41 REMARK 500 3 ASP A 46 -34.96 169.66 REMARK 500 3 TYR A 49 140.04 -32.27 REMARK 500 3 PHE A 50 -44.94 -154.83 REMARK 500 3 THR A 62 -153.42 -67.83 REMARK 500 3 LEU A 63 -71.52 -100.26 REMARK 500 3 ASP A 64 -9.52 -57.90 REMARK 500 3 LEU A 66 -40.68 -171.69 REMARK 500 3 THR A 67 153.78 -42.60 REMARK 500 3 ASN A 75 -59.45 -148.50 REMARK 500 3 TYR A 89 162.18 160.26 REMARK 500 3 PRO A 90 -90.72 -75.05 REMARK 500 REMARK 500 THIS ENTRY HAS 347 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: ET99 RELATED DB: TARGETDB DBREF 1TE7 A 1 103 UNP P67603 YQFB_ECOLI 1 103 SEQRES 1 A 103 MET GLN PRO ASN ASP ILE THR PHE PHE GLN ARG PHE GLN SEQRES 2 A 103 ASP ASP ILE LEU ALA GLY ARG LYS THR ILE THR ILE ARG SEQRES 3 A 103 ASP GLU SER GLU SER HIS PHE LYS THR GLY ASP VAL LEU SEQRES 4 A 103 ARG VAL GLY ARG PHE GLU ASP ASP GLY TYR PHE CYS THR SEQRES 5 A 103 ILE GLU VAL THR ALA THR SER THR VAL THR LEU ASP THR SEQRES 6 A 103 LEU THR GLU LYS HIS ALA GLU GLN GLU ASN MET THR LEU SEQRES 7 A 103 THR GLU LEU LYS LYS VAL ILE ALA ASP ILE TYR PRO GLY SEQRES 8 A 103 GLN THR GLN PHE TYR VAL ILE GLU PHE LYS CYS LEU HELIX 1 1 PHE A 9 ALA A 18 1 10 HELIX 2 2 ASP A 27 SER A 31 5 5 HELIX 3 3 GLU A 68 GLU A 74 1 7 HELIX 4 4 THR A 77 TYR A 89 1 13 SHEET 1 A 4 THR A 22 ARG A 26 0 SHEET 2 A 4 PHE A 95 LYS A 101 -1 O TYR A 96 N ARG A 26 SHEET 3 A 4 ASP A 47 VAL A 61 -1 N SER A 59 O VAL A 97 SHEET 4 A 4 VAL A 38 ARG A 43 -1 N LEU A 39 O ILE A 53 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