Header list of 1zwt.pdb file
Complete list - r 25 2 Bytes
HEADER CELL ADHESION 06-JUN-05 1ZWT TITLE STRUCTURE OF THE GLOBULAR HEAD DOMAIN OF THE BUNDLIN, BFPA, OF THE TITLE 2 BUNDLE-FORMING PILUS OF ENTEROPATHOGENIC E.COLI COMPND MOL_ID: 1; COMPND 2 MOLECULE: MAJOR STRUCTURAL SUBUNIT OF BUNDLE-FORMING PILUS; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: BFPA; COMPND 5 SYNONYM: BUNDLE- FORMING PILIN, BUNDLIN, BFP; COMPND 6 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI; SOURCE 3 ORGANISM_TAXID: 168807; SOURCE 4 STRAIN: O127:H6; SOURCE 5 GENE: BFPA; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: RY3080; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET39B+ KEYWDS ALPHA-BETA FOLD, BETA-SANDWICH, ONE DISULFIDE BOND, CELL ADHESION EXPDTA SOLUTION NMR NUMMDL 12 AUTHOR S.RAMBOARINA,P.J.FERNANDES,S.DANIELL,S.ISLAM,G.FRANKEL,F.BOOY, AUTHOR 2 M.S.DONNENBERG,S.MATTHEWS REVDAT 4 13-JUL-11 1ZWT 1 VERSN REVDAT 3 24-FEB-09 1ZWT 1 VERSN REVDAT 2 06-DEC-05 1ZWT 1 JRNL REVDAT 1 04-OCT-05 1ZWT 0 JRNL AUTH S.RAMBOARINA,P.J.FERNANDES,S.DANIELL,S.ISLAM,P.SIMPSON, JRNL AUTH 2 G.FRANKEL,F.BOOY,M.S.DONNENBERG,S.MATTHEWS JRNL TITL STRUCTURE OF THE BUNDLE-FORMING PILUS FROM ENTEROPATHOGENIC JRNL TITL 2 ESCHERICHIA COLI JRNL REF J.BIOL.CHEM. V. 280 40252 2005 JRNL REFN ISSN 0021-9258 JRNL PMID 16172128 JRNL DOI 10.1074/JBC.M508099200 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH S.RAMBOARINA,P.FERNANDES,P.SIMPSON,G.FRANKEL,M.DONNENBERG, REMARK 1 AUTH 2 S.MATTHEWS REMARK 1 TITL COMPLETE RESONANCE ASSIGNMENTS OF BUNDLIN (BFPA) FROM THE REMARK 1 TITL 2 BUNDLE-FORMING PILUS OF ENTEROPATHOGENIC ESCHERICHIA COLI REMARK 1 REF J.BIOMOL.NMR V. 29 427 2004 REMARK 1 REFN ISSN 0925-2738 REMARK 1 PMID 15213452 REMARK 1 DOI 10.1023/B:JNMR.0000032511.89525.64 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : ARIA 1.2 REMARK 3 AUTHORS : LINGE AND NILGES REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REMARK 3 577 AMBIGUOUS AND 2277 UNAMBIGUOUS NOE RESTRAINTS, REMARK 3 86 TALOS CONSTRAINTS AND 38 HYDROGEN BONDS WERE IMPOSED REMARK 3 DURING ARIA STRUCTURE CALCULATIONS. REMARK 4 REMARK 4 1ZWT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-JUN-05. REMARK 100 THE RCSB ID CODE IS RCSB033209. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 303 REMARK 210 PH : 5.2 REMARK 210 IONIC STRENGTH : NO SALT REMARK 210 PRESSURE : NORMAL REMARK 210 SAMPLE CONTENTS : 0.5 MM BFPA U-15N,13C, 20 MM REMARK 210 SODIUM PHOSPHATE BUFFER PH 5.2, REMARK 210 90%H20, 10% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N- REMARK 210 SEPARATED_NOESY; 3D HBHA(CBCACO) REMARK 210 NH; 3D H(C)CH-TOCSY; 3D (H)CC(CO) REMARK 210 NH-TOCSY REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 800 MHZ REMARK 210 SPECTROMETER MODEL : DRX; INOVA REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRPIPE, NMRVIEW 5.0.4 REMARK 210 METHOD USED : SIMULATED ANNEALING WITH NMR REMARK 210 RESTRAINTS USING ARIA REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 12 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH ACCEPTABLE REMARK 210 COVALENT GEOMETRY, STRUCTURES REMARK 210 WITH THE LEAST RESTRAINT REMARK 210 VIOLATIONS, STRUCTURES WITH THE REMARK 210 LOWEST ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 12 REMARK 210 REMARK 210 REMARK: HYDROGEN-EXCHANGE EXPERIMENTS 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 HB2 ALA A 126 HZ3 LYS A 131 1.14 REMARK 500 HA LYS A 59 HB2 LEU A 89 1.27 REMARK 500 HB2 ASP A 55 HB2 LYS A 60 1.35 REMARK 500 HZ PHE A 80 HE2 PHE A 122 1.40 REMARK 500 H GLY A 67 HD21 LEU A 86 1.41 REMARK 500 HG22 THR A 62 HG2 GLU A 116 1.42 REMARK 500 HA ALA A 106 H LYS A 158 1.45 REMARK 500 HA LEU A 44 HA ALA A 48 1.47 REMARK 500 HA3 GLY A 103 HG22 THR A 133 1.54 REMARK 500 O ILE A 135 HG1 THR A 136 1.54 REMARK 500 HG1 THR A 62 OE2 GLU A 116 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 GLU A 2 90.73 57.86 REMARK 500 1 GLN A 3 -172.57 67.14 REMARK 500 1 ALA A 5 -54.43 69.91 REMARK 500 1 ILE A 30 63.01 68.25 REMARK 500 1 THR A 33 -58.10 70.18 REMARK 500 1 SER A 34 50.88 -170.34 REMARK 500 1 SER A 47 13.98 59.77 REMARK 500 1 ALA A 48 -35.00 68.07 REMARK 500 1 TYR A 53 -8.62 -59.87 REMARK 500 1 ASN A 58 13.96 160.09 REMARK 500 1 ASN A 63 -55.74 170.99 REMARK 500 1 PHE A 65 28.07 -145.32 REMARK 500 1 ARG A 88 127.55 164.35 REMARK 500 1 ASN A 124 19.26 -143.29 REMARK 500 1 ASP A 127 103.27 69.71 REMARK 500 1 ILE A 135 164.54 179.79 REMARK 500 1 THR A 136 153.25 66.20 REMARK 500 1 ASP A 148 -69.36 -125.85 REMARK 500 2 GLU A 2 78.99 61.65 REMARK 500 2 GLN A 3 21.02 -154.49 REMARK 500 2 ALA A 5 -55.50 72.35 REMARK 500 2 SER A 8 -55.22 -124.67 REMARK 500 2 ILE A 30 108.81 68.86 REMARK 500 2 THR A 33 -58.67 70.69 REMARK 500 2 SER A 34 27.69 -153.10 REMARK 500 2 SER A 47 25.51 45.15 REMARK 500 2 ALA A 48 -39.30 68.55 REMARK 500 2 PRO A 50 99.13 -63.82 REMARK 500 2 ASN A 58 14.54 158.57 REMARK 500 2 ASN A 63 -50.97 160.84 REMARK 500 2 ASN A 75 -78.46 62.04 REMARK 500 2 ARG A 88 122.64 160.14 REMARK 500 2 LEU A 102 38.43 -81.83 REMARK 500 2 THR A 104 -54.46 -122.26 REMARK 500 2 ASN A 118 73.45 -153.28 REMARK 500 2 ASN A 124 37.73 -145.01 REMARK 500 2 ASP A 127 92.92 74.51 REMARK 500 2 ILE A 135 18.31 175.58 REMARK 500 2 ALA A 143 -70.70 -61.01 REMARK 500 2 LYS A 145 -83.17 -93.13 REMARK 500 2 ASP A 148 -84.82 -110.29 REMARK 500 2 MET A 157 79.43 -118.53 REMARK 500 3 GLU A 2 101.73 69.13 REMARK 500 3 GLN A 3 -174.70 61.88 REMARK 500 3 GLN A 32 -71.71 -115.82 REMARK 500 3 THR A 33 -37.66 68.59 REMARK 500 3 TYR A 35 -18.49 77.35 REMARK 500 3 SER A 36 8.87 51.16 REMARK 500 3 LEU A 38 24.78 46.58 REMARK 500 3 SER A 47 84.68 -26.86 REMARK 500 REMARK 500 THIS ENTRY HAS 196 RAMACHANDRAN OUTLIERS. 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 4 TYR A 109 0.05 SIDE CHAIN REMARK 500 7 TYR A 155 0.05 SIDE CHAIN REMARK 500 8 TYR A 35 0.06 SIDE CHAIN REMARK 500 10 TYR A 155 0.05 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 6003 RELATED DB: BMRB DBREF 1ZWT A 3 158 UNP P33553 BFPA_ECO27 38 193 SEQADV 1ZWT MET A 1 UNP P33553 CLONING ARTIFACT SEQADV 1ZWT GLU A 2 UNP P33553 CLONING ARTIFACT SEQRES 1 A 158 MET GLU GLN SER ALA SER ASP SER ASN LYS SER GLN ASN SEQRES 2 A 158 ALA ILE SER GLU VAL MET SER ALA THR SER ALA ILE ASN SEQRES 3 A 158 GLY LEU TYR ILE GLY GLN THR SER TYR SER GLY LEU ASP SEQRES 4 A 158 SER THR ILE LEU LEU ASN THR SER ALA ILE PRO ASP ASN SEQRES 5 A 158 TYR LYS ASP THR THR ASN LYS LYS ILE THR ASN PRO PHE SEQRES 6 A 158 GLY GLY GLU LEU ASN VAL GLY PRO ALA ASN ASN ASN THR SEQRES 7 A 158 ALA PHE GLY TYR TYR LEU THR LEU THR ARG LEU ASP LYS SEQRES 8 A 158 ALA ALA CYS VAL SER LEU ALA THR LEU ASN LEU GLY THR SEQRES 9 A 158 SER ALA LYS GLY TYR GLY VAL ASN ILE SER GLY GLU ASN SEQRES 10 A 158 ASN ILE THR SER PHE GLY ASN SER ALA ASP GLN ALA ALA SEQRES 11 A 158 LYS SER THR ALA ILE THR PRO ALA GLU ALA ALA THR ALA SEQRES 12 A 158 CYS LYS ASN THR ASP SER THR ASN LYS VAL THR TYR PHE SEQRES 13 A 158 MET LYS HELIX 1 1 SER A 8 ILE A 30 1 23 HELIX 2 2 GLY A 31 SER A 36 1 6 HELIX 3 3 GLY A 37 THR A 46 1 10 HELIX 4 4 PRO A 50 LYS A 54 5 5 HELIX 5 5 ASP A 90 THR A 99 1 10 HELIX 6 6 GLY A 115 ILE A 119 5 5 HELIX 7 7 ILE A 135 CYS A 144 1 10 SHEET 1 A 7 VAL A 71 PRO A 73 0 SHEET 2 A 7 TYR A 82 LEU A 86 -1 O TYR A 83 N GLY A 72 SHEET 3 A 7 ILE A 61 THR A 62 -1 N ILE A 61 O LEU A 86 SHEET 4 A 7 VAL A 153 PHE A 156 1 O TYR A 155 N THR A 62 SHEET 5 A 7 GLY A 108 VAL A 111 -1 N GLY A 108 O PHE A 156 SHEET 6 A 7 ALA A 129 LYS A 131 -1 O LYS A 131 N TYR A 109 SHEET 7 A 7 PHE A 122 GLY A 123 1 N GLY A 123 O ALA A 130 SSBOND 1 CYS A 94 CYS A 144 1555 1555 2.03 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 25 2 Bytes