Header list of 1bf8.pdb file
Complete list - b 16 2 Bytes
HEADER CHAPERONE 28-MAY-98 1BF8 TITLE PERIPLASMIC CHAPERONE FIMC, NMR, 20 STRUCTURES COMPND MOL_ID: 1; COMPND 2 MOLECULE: CHAPERONE PROTEIN FIMC; 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 CELL_LINE: BL21; SOURCE 5 CELLULAR_LOCATION: PERIPLASM; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3); SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PFIMC KEYWDS CHAPERONE, FIMC, PERIPLASMIC CHAPERONE, PILUS CHAPERONE, TYPE-I PILI EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR M.PELLECCHIA,P.GUNTERT,R.GLOCKSHUBER,K.WUTHRICH REVDAT 3 16-FEB-22 1BF8 1 REMARK REVDAT 2 24-FEB-09 1BF8 1 VERSN REVDAT 1 18-NOV-98 1BF8 0 JRNL AUTH M.PELLECCHIA,P.GUNTERT,R.GLOCKSHUBER,K.WUTHRICH JRNL TITL NMR SOLUTION STRUCTURE OF THE PERIPLASMIC CHAPERONE FIMC. JRNL REF NAT.STRUCT.BIOL. V. 5 885 1998 JRNL REFN ISSN 1072-8368 JRNL PMID 9783748 JRNL DOI 10.1038/2325 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH M.PELLECCHIA,P.GUNTERT,R.GLOCKSHUBER,K.WUTHRICH REMARK 1 TITL SEQUENCE-SPECIFIC 1H, 15N, AND 13C ASSIGNMENTS OF THE REMARK 1 TITL 2 PERIPLASMIC CHAPERONE FIMC FROM ESCHERICHIA COLI REMARK 1 REF J.BIOMOL.NMR V. 11 229 1998 REMARK 1 REFN ISSN 0925-2738 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : DYANA REMARK 3 AUTHORS : LUGINBUHL, GUNTERT, BILLETER,WUTHRICH REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1BF8 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL. REMARK 100 THE DEPOSITION ID IS D_1000171684. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 311 REMARK 210 PH : 5.0 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : SEE PAPER REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ REMARK 210 SPECTROMETER MODEL : UNITY REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : DYANA REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 80 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 11 REMARK 210 REMARK 210 REMARK: SEE JRNL ARTICLE FOR DETAILS 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 HG1 THR A 159 OD2 ASP A 180 1.60 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 10 TYR A 11 CB - CG - CD2 ANGL. DEV. = -3.7 DEGREES REMARK 500 17 TYR A 11 CB - CG - CD2 ANGL. DEV. = -4.4 DEGREES REMARK 500 17 ARG A 188 NE - CZ - NH2 ANGL. DEV. = -3.2 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 VAL A 2 145.00 62.78 REMARK 500 1 ALA A 3 77.40 -109.15 REMARK 500 1 TYR A 11 75.39 -118.29 REMARK 500 1 ALA A 13 64.12 33.18 REMARK 500 1 LYS A 16 -103.97 163.02 REMARK 500 1 ALA A 40 -5.80 55.18 REMARK 500 1 THR A 71 -83.82 -74.79 REMARK 500 1 ASN A 72 15.04 53.41 REMARK 500 1 PRO A 91 83.21 -69.29 REMARK 500 1 SER A 92 98.29 62.39 REMARK 500 1 LEU A 98 65.54 35.16 REMARK 500 1 GLU A 100 -164.17 52.72 REMARK 500 1 LEU A 105 107.72 -59.37 REMARK 500 1 ALA A 106 96.04 -178.27 REMARK 500 1 ARG A 110 87.44 40.04 REMARK 500 1 ARG A 116 109.60 -161.31 REMARK 500 1 ALA A 137 39.36 -81.84 REMARK 500 1 ASN A 138 -28.20 -172.25 REMARK 500 1 ASN A 144 56.40 -118.19 REMARK 500 1 PRO A 145 20.47 -79.48 REMARK 500 1 GLU A 154 64.57 63.33 REMARK 500 1 SER A 179 34.43 -76.76 REMARK 500 1 ASP A 180 -76.17 -128.49 REMARK 500 1 ALA A 181 93.95 33.03 REMARK 500 2 VAL A 2 125.30 73.33 REMARK 500 2 LEU A 4 166.12 54.09 REMARK 500 2 ALA A 13 167.04 64.51 REMARK 500 2 GLN A 15 43.42 36.34 REMARK 500 2 GLN A 17 146.04 77.60 REMARK 500 2 THR A 71 -78.49 -69.95 REMARK 500 2 ASN A 72 -2.97 56.83 REMARK 500 2 ASN A 73 27.20 -79.87 REMARK 500 2 GLN A 74 71.84 44.35 REMARK 500 2 SER A 92 81.38 41.82 REMARK 500 2 LYS A 95 91.33 56.95 REMARK 500 2 SER A 96 54.27 -144.94 REMARK 500 2 LEU A 98 78.64 73.73 REMARK 500 2 THR A 99 63.28 33.87 REMARK 500 2 ASN A 101 23.05 -157.91 REMARK 500 2 LEU A 105 127.69 58.05 REMARK 500 2 ARG A 110 128.02 60.63 REMARK 500 2 PRO A 117 7.35 -69.47 REMARK 500 2 GLU A 154 63.72 62.30 REMARK 500 2 PRO A 178 30.95 -87.07 REMARK 500 2 SER A 179 23.79 48.84 REMARK 500 2 ASP A 180 -76.88 -122.33 REMARK 500 2 ALA A 181 80.48 33.49 REMARK 500 2 LEU A 196 109.49 -25.21 REMARK 500 2 THR A 201 -179.16 -65.62 REMARK 500 3 VAL A 2 156.79 54.89 REMARK 500 REMARK 500 THIS ENTRY HAS 397 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 GLY A 1 VAL A 2 2 -149.34 REMARK 500 GLY A 1 VAL A 2 3 -145.62 REMARK 500 GLY A 1 VAL A 2 15 144.50 REMARK 500 GLY A 1 VAL A 2 16 -149.61 REMARK 500 GLY A 1 VAL A 2 19 -141.88 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 47 0.13 SIDE CHAIN REMARK 500 1 TYR A 149 0.08 SIDE CHAIN REMARK 500 2 ARG A 79 0.08 SIDE CHAIN REMARK 500 2 TYR A 115 0.06 SIDE CHAIN REMARK 500 2 TYR A 148 0.10 SIDE CHAIN REMARK 500 2 ARG A 160 0.08 SIDE CHAIN REMARK 500 3 TYR A 115 0.07 SIDE CHAIN REMARK 500 3 ARG A 160 0.08 SIDE CHAIN REMARK 500 4 ARG A 47 0.11 SIDE CHAIN REMARK 500 4 TYR A 114 0.09 SIDE CHAIN REMARK 500 5 ARG A 135 0.12 SIDE CHAIN REMARK 500 6 ARG A 8 0.12 SIDE CHAIN REMARK 500 6 ARG A 79 0.08 SIDE CHAIN REMARK 500 6 TYR A 149 0.09 SIDE CHAIN REMARK 500 7 ARG A 134 0.08 SIDE CHAIN REMARK 500 7 TYR A 148 0.07 SIDE CHAIN REMARK 500 7 ARG A 188 0.12 SIDE CHAIN REMARK 500 8 ARG A 79 0.08 SIDE CHAIN REMARK 500 8 TYR A 114 0.09 SIDE CHAIN REMARK 500 8 TYR A 149 0.07 SIDE CHAIN REMARK 500 10 ARG A 8 0.08 SIDE CHAIN REMARK 500 10 TYR A 115 0.08 SIDE CHAIN REMARK 500 10 TYR A 148 0.11 SIDE CHAIN REMARK 500 11 PHE A 133 0.08 SIDE CHAIN REMARK 500 11 TYR A 149 0.10 SIDE CHAIN REMARK 500 12 ARG A 47 0.08 SIDE CHAIN REMARK 500 12 ARG A 110 0.11 SIDE CHAIN REMARK 500 12 ARG A 135 0.09 SIDE CHAIN REMARK 500 13 ARG A 116 0.11 SIDE CHAIN REMARK 500 13 ARG A 134 0.08 SIDE CHAIN REMARK 500 13 TYR A 148 0.07 SIDE CHAIN REMARK 500 13 TYR A 149 0.11 SIDE CHAIN REMARK 500 13 ARG A 160 0.08 SIDE CHAIN REMARK 500 13 ARG A 188 0.22 SIDE CHAIN REMARK 500 14 ARG A 66 0.17 SIDE CHAIN REMARK 500 14 ARG A 116 0.09 SIDE CHAIN REMARK 500 14 ARG A 135 0.09 SIDE CHAIN REMARK 500 14 TYR A 149 0.10 SIDE CHAIN REMARK 500 15 ARG A 79 0.08 SIDE CHAIN REMARK 500 17 ARG A 8 0.10 SIDE CHAIN REMARK 500 18 ARG A 110 0.09 SIDE CHAIN REMARK 500 19 TYR A 114 0.10 SIDE CHAIN REMARK 500 19 ARG A 116 0.18 SIDE CHAIN REMARK 500 19 ARG A 135 0.08 SIDE CHAIN REMARK 500 19 TYR A 149 0.08 SIDE CHAIN REMARK 500 19 ARG A 160 0.09 SIDE CHAIN REMARK 500 20 TYR A 193 0.07 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL DBREF 1BF8 A 1 205 UNP P31697 FIMC_ECOLI 37 241 SEQRES 1 A 205 GLY VAL ALA LEU GLY ALA THR ARG VAL ILE TYR PRO ALA SEQRES 2 A 205 GLY GLN LYS GLN GLU GLN LEU ALA VAL THR ASN ASN ASP SEQRES 3 A 205 GLU ASN SER THR TYR LEU ILE GLN SER TRP VAL GLU ASN SEQRES 4 A 205 ALA ASP GLY VAL LYS ASP GLY ARG PHE ILE VAL THR PRO SEQRES 5 A 205 PRO LEU PHE ALA MET LYS GLY LYS LYS GLU ASN THR LEU SEQRES 6 A 205 ARG ILE LEU ASP ALA THR ASN ASN GLN LEU PRO GLN ASP SEQRES 7 A 205 ARG GLU SER LEU PHE TRP MET ASN VAL LYS ALA ILE PRO SEQRES 8 A 205 SER MET ASP LYS SER LYS LEU THR GLU ASN THR LEU GLN SEQRES 9 A 205 LEU ALA ILE ILE SER ARG ILE LYS LEU TYR TYR ARG PRO SEQRES 10 A 205 ALA LYS LEU ALA LEU PRO PRO ASP GLN ALA ALA GLU LYS SEQRES 11 A 205 LEU ARG PHE ARG ARG SER ALA ASN SER LEU THR LEU ILE SEQRES 12 A 205 ASN PRO THR PRO TYR TYR LEU THR VAL THR GLU LEU ASN SEQRES 13 A 205 ALA GLY THR ARG VAL LEU GLU ASN ALA LEU VAL PRO PRO SEQRES 14 A 205 MET GLY GLU SER THR VAL LYS LEU PRO SER ASP ALA GLY SEQRES 15 A 205 SER ASN ILE THR TYR ARG THR ILE ASN ASP TYR GLY ALA SEQRES 16 A 205 LEU THR PRO LYS MET THR GLY VAL MET GLU HELIX 1 H1 GLN A 126 LYS A 130 3 5 SHEET 1 S1 4 VAL A 2 ALA A 6 0 SHEET 2 S1 4 GLN A 17 ASN A 24 -1 SHEET 3 S1 4 LYS A 61 LEU A 68 -1 SHEET 4 S1 4 PHE A 48 THR A 51 -1 SHEET 1 S2 5 LEU A 54 GLY A 59 0 SHEET 2 S2 5 THR A 30 GLU A 38 -1 SHEET 3 S2 5 SER A 81 SER A 92 -1 SHEET 4 S2 5 ALA A 106 TYR A 115 -1 SHEET 5 S2 5 ARG A 8 ALA A 13 1 SHEET 1 S3 3 ARG A 132 SER A 136 0 SHEET 2 S3 3 ASN A 138 PRO A 145 -1 SHEET 3 S3 3 MET A 170 LEU A 177 -1 SHEET 1 S4 4 ARG A 160 VAL A 167 0 SHEET 2 S4 4 TYR A 149 GLY A 158 -1 SHEET 3 S4 4 GLY A 182 TYR A 193 -1 SHEET 4 S4 4 ALA A 195 GLY A 202 -1 CISPEP 1 THR A 51 PRO A 52 1 -11.10 CISPEP 2 THR A 51 PRO A 52 2 -11.23 CISPEP 3 THR A 51 PRO A 52 3 -17.72 CISPEP 4 THR A 51 PRO A 52 4 -20.70 CISPEP 5 THR A 51 PRO A 52 5 -19.29 CISPEP 6 THR A 51 PRO A 52 6 -15.67 CISPEP 7 THR A 51 PRO A 52 7 -20.30 CISPEP 8 THR A 51 PRO A 52 8 -17.41 CISPEP 9 THR A 51 PRO A 52 9 -18.95 CISPEP 10 THR A 51 PRO A 52 10 -20.67 CISPEP 11 THR A 51 PRO A 52 11 -18.42 CISPEP 12 THR A 51 PRO A 52 12 -1.55 CISPEP 13 THR A 51 PRO A 52 13 -18.80 CISPEP 14 THR A 51 PRO A 52 14 -21.14 CISPEP 15 THR A 51 PRO A 52 15 -20.04 CISPEP 16 THR A 51 PRO A 52 16 -20.76 CISPEP 17 THR A 51 PRO A 52 17 -20.60 CISPEP 18 THR A 51 PRO A 52 18 -21.16 CISPEP 19 THR A 51 PRO A 52 19 -17.09 CISPEP 20 THR A 51 PRO A 52 20 -21.02 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 - b 16 2 Bytes