Header list of 1cye.pdb file
Complete list - t 16 2 Bytes
HEADER SIGNAL TRANSDUCTION 21-OCT-94 1CYE TITLE THREE DIMENSIONAL STRUCTURE OF CHEMOTACTIC CHE Y PROTEIN IN AQUEOUS TITLE 2 SOLUTION BY NUCLEAR MAGNETIC RESONANCE METHODS COMPND MOL_ID: 1; COMPND 2 MOLECULE: CHEY; 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 EXPRESSION_SYSTEM_PLASMID: CHEY KEYWDS SIGNAL TRANSDUCTION EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR J.SANTORO,M.BRUIX,J.PASCUAL,E.LOPEZ,L.SERRANO,M.RICO REVDAT 3 16-OCT-19 1CYE 1 JRNL REMARK REVDAT 2 24-FEB-09 1CYE 1 VERSN REVDAT 1 07-FEB-95 1CYE 0 JRNL AUTH J.SANTORO,M.BRUIX,J.PASCUAL,E.LOPEZ,L.SERRANO,M.RICO JRNL TITL THREE-DIMENSIONAL STRUCTURE OF CHEMOTACTIC CHE Y PROTEIN IN JRNL TITL 2 AQUEOUS SOLUTION BY NUCLEAR MAGNETIC RESONANCE METHODS. JRNL REF J.MOL.BIOL. V. 247 717 1995 JRNL REFN ESSN 1089-8638 JRNL PMID 7723026 JRNL DOI 10.1016/S0022-2836(05)80150-0 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH M.BRUIX,J.PASCUAL,J.SANTORO,J.PRIETO,L.SERRANO,M.RICO REMARK 1 TITL 1H AND 15N-NMR ASSIGNMENT AND SOLUTION STRUCTURE OF THE REMARK 1 TITL 2 CHEMOTACTIC ESCHERICHIA COLI CHE Y PROTEIN REMARK 1 REF EUR.J.BIOCHEM. V. 215 573 1993 REMARK 1 REFN ISSN 0014-2956 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : DIANA, GROMOS REMARK 3 AUTHORS : GUNTERT,BRAUN,WUTHRICH (DIANA), VAN REMARK 3 GUNSTEREN,BERENDSEN (GROMOS) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1CYE 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_1000172597. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : NULL REMARK 210 PH : NULL REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL REMARK 210 SPECTROMETER FIELD STRENGTH : NULL REMARK 210 SPECTROMETER MODEL : NULL REMARK 210 SPECTROMETER MANUFACTURER : NULL REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NULL REMARK 210 METHOD USED : NULL REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL 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 1 ARG A 1 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES REMARK 500 3 TYR A 51 CB - CG - CD2 ANGL. DEV. = -5.4 DEGREES REMARK 500 4 TYR A 51 CB - CG - CD2 ANGL. DEV. = -3.7 DEGREES REMARK 500 9 PHE A 8 CB - CG - CD1 ANGL. DEV. = -4.2 DEGREES REMARK 500 14 ARG A 19 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES REMARK 500 16 TYR A 51 CB - CG - CD2 ANGL. DEV. = -6.7 DEGREES REMARK 500 19 ARG A 19 NE - CZ - NH1 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 LYS A 4 -32.73 70.55 REMARK 500 1 PHE A 53 144.06 -174.29 REMARK 500 1 ASN A 62 -64.08 68.90 REMARK 500 2 GLU A 5 73.29 -118.80 REMARK 500 2 PHE A 53 129.49 -178.72 REMARK 500 2 ASN A 62 -72.92 70.31 REMARK 500 3 PHE A 53 129.26 -178.13 REMARK 500 3 ASN A 62 -65.02 69.69 REMARK 500 4 SER A 2 20.01 -74.14 REMARK 500 4 ASP A 3 77.65 -117.25 REMARK 500 4 PHE A 53 131.52 -178.71 REMARK 500 4 ASN A 62 -69.51 70.47 REMARK 500 4 SER A 79 -61.03 2.57 REMARK 500 5 GLU A 5 41.10 -100.07 REMARK 500 5 VAL A 11 60.32 -108.24 REMARK 500 5 ASP A 13 -42.58 -13.58 REMARK 500 5 SER A 15 27.26 -65.98 REMARK 500 5 THR A 16 -58.52 -123.72 REMARK 500 5 ASN A 62 -69.81 67.89 REMARK 500 5 SER A 79 -78.21 8.82 REMARK 500 5 ALA A 80 29.25 -77.03 REMARK 500 5 GLU A 89 118.79 -166.74 REMARK 500 5 LEU A 127 36.43 -90.65 REMARK 500 6 GLU A 5 50.93 -91.27 REMARK 500 6 PHE A 14 115.09 172.25 REMARK 500 6 PHE A 53 140.08 -172.41 REMARK 500 6 ASN A 62 -79.68 70.82 REMARK 500 6 ALA A 90 55.83 -94.10 REMARK 500 7 ASN A 62 -72.36 66.84 REMARK 500 7 ILE A 72 -62.02 -109.64 REMARK 500 7 LYS A 92 -61.11 -25.95 REMARK 500 8 ASP A 3 -31.22 -38.26 REMARK 500 8 GLU A 5 9.03 -66.77 REMARK 500 8 ASN A 62 -76.25 99.17 REMARK 500 8 ILE A 72 -65.46 -96.31 REMARK 500 8 SER A 79 39.19 -58.64 REMARK 500 9 GLU A 5 54.41 -96.95 REMARK 500 9 ASN A 62 -66.64 65.12 REMARK 500 9 SER A 79 -35.92 -30.00 REMARK 500 10 ASN A 62 -61.20 71.19 REMARK 500 11 VAL A 11 72.56 -104.44 REMARK 500 11 ASP A 13 -30.61 -13.01 REMARK 500 11 ASN A 62 -67.32 63.75 REMARK 500 11 SER A 79 -36.07 -38.03 REMARK 500 12 LYS A 4 -69.34 -151.88 REMARK 500 12 ASN A 62 -65.80 81.32 REMARK 500 12 LYS A 92 -61.63 -25.50 REMARK 500 13 SER A 2 -30.78 61.66 REMARK 500 13 LYS A 4 -51.97 -133.18 REMARK 500 13 PHE A 53 137.03 -171.05 REMARK 500 REMARK 500 THIS ENTRY HAS 85 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 1 TYR A 106 0.09 SIDE CHAIN REMARK 500 1 PHE A 124 0.07 SIDE CHAIN REMARK 500 2 TYR A 51 0.06 SIDE CHAIN REMARK 500 3 TYR A 51 0.08 SIDE CHAIN REMARK 500 4 TYR A 51 0.15 SIDE CHAIN REMARK 500 5 PHE A 124 0.09 SIDE CHAIN REMARK 500 7 TYR A 51 0.08 SIDE CHAIN REMARK 500 8 TYR A 51 0.10 SIDE CHAIN REMARK 500 9 TYR A 51 0.06 SIDE CHAIN REMARK 500 9 PHE A 124 0.08 SIDE CHAIN REMARK 500 13 TYR A 51 0.12 SIDE CHAIN REMARK 500 13 PHE A 124 0.09 SIDE CHAIN REMARK 500 16 TYR A 51 0.15 SIDE CHAIN REMARK 500 17 ARG A 1 0.08 SIDE CHAIN REMARK 500 17 PHE A 8 0.08 SIDE CHAIN REMARK 500 17 PHE A 124 0.08 SIDE CHAIN REMARK 500 18 ARG A 1 0.09 SIDE CHAIN REMARK 500 18 PHE A 8 0.08 SIDE CHAIN REMARK 500 18 TYR A 51 0.11 SIDE CHAIN REMARK 500 19 ARG A 1 0.08 SIDE CHAIN REMARK 500 19 PHE A 14 0.08 SIDE CHAIN REMARK 500 19 TYR A 51 0.10 SIDE CHAIN REMARK 500 19 PHE A 124 0.08 SIDE CHAIN REMARK 500 20 ARG A 18 0.08 SIDE CHAIN REMARK 500 20 ARG A 19 0.10 SIDE CHAIN REMARK 500 20 TYR A 51 0.13 SIDE CHAIN REMARK 500 20 PHE A 124 0.09 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY REMARK 500 REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 500 I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI ANGLE REMARK 500 15 LEU A 127 10.36 REMARK 500 16 TYR A 51 -10.41 REMARK 500 REMARK 500 REMARK: NULL DBREF 1CYE A 3 129 UNP P06143 CHEY_ECOLI 2 128 SEQRES 1 A 129 ARG SER ASP LYS GLU LEU LYS PHE LEU VAL VAL ASP ASP SEQRES 2 A 129 PHE SER THR MET ARG ARG ILE VAL ARG ASN LEU LEU LYS SEQRES 3 A 129 GLU LEU GLY PHE ASN ASN VAL GLU GLU ALA GLU ASP GLY SEQRES 4 A 129 VAL ASP ALA LEU ASN LYS LEU GLN ALA GLY GLY TYR GLY SEQRES 5 A 129 PHE VAL ILE SER ASP TRP ASN MET PRO ASN MET ASP GLY SEQRES 6 A 129 LEU GLU LEU LEU LYS THR ILE ARG ALA ASP GLY ALA MET SEQRES 7 A 129 SER ALA LEU PRO VAL LEU MET VAL THR ALA GLU ALA LYS SEQRES 8 A 129 LYS GLU ASN ILE ILE ALA ALA ALA GLN ALA GLY ALA SER SEQRES 9 A 129 GLY TYR VAL VAL LYS PRO PHE THR ALA ALA THR LEU GLU SEQRES 10 A 129 GLU LYS LEU ASN LYS ILE PHE GLU LYS LEU GLY MET HELIX 1 1 PHE A 14 LEU A 28 1 15 HELIX 2 2 ASP A 38 ALA A 48 1 11 HELIX 3 3 ASP A 64 ASP A 75 1 12 HELIX 4 4 GLY A 76 LEU A 81 5 6 HELIX 5 5 LYS A 91 ALA A 101 1 11 HELIX 6 6 THR A 112 GLY A 128 1 17 SHEET 1 A 5 VAL A 33 ALA A 36 0 SHEET 2 A 5 PHE A 8 VAL A 11 1 O PHE A 8 N GLU A 34 SHEET 3 A 5 PHE A 53 ASP A 57 1 O PHE A 53 N LEU A 9 SHEET 4 A 5 VAL A 83 THR A 87 1 N LEU A 84 O VAL A 54 SHEET 5 A 5 GLY A 105 VAL A 108 1 O GLY A 105 N MET A 85 CISPEP 1 LYS A 109 PRO A 110 1 -0.68 CISPEP 2 LYS A 109 PRO A 110 2 0.64 CISPEP 3 LYS A 109 PRO A 110 3 -1.24 CISPEP 4 LYS A 109 PRO A 110 4 0.89 CISPEP 5 LYS A 109 PRO A 110 5 0.21 CISPEP 6 LYS A 109 PRO A 110 6 0.47 CISPEP 7 LYS A 109 PRO A 110 7 -2.02 CISPEP 8 LYS A 109 PRO A 110 8 -0.67 CISPEP 9 LYS A 109 PRO A 110 9 0.17 CISPEP 10 LYS A 109 PRO A 110 10 0.33 CISPEP 11 LYS A 109 PRO A 110 11 0.81 CISPEP 12 LYS A 109 PRO A 110 12 0.40 CISPEP 13 LYS A 109 PRO A 110 13 0.37 CISPEP 14 LYS A 109 PRO A 110 14 0.90 CISPEP 15 LYS A 109 PRO A 110 15 -0.30 CISPEP 16 LYS A 109 PRO A 110 16 1.00 CISPEP 17 LYS A 109 PRO A 110 17 0.97 CISPEP 18 LYS A 109 PRO A 110 18 0.24 CISPEP 19 LYS A 109 PRO A 110 19 0.40 CISPEP 20 LYS A 109 PRO A 110 20 -0.27 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 - t 16 2 Bytes