Header list of 1rcs.pdb file
Complete list - r 2 2 Bytes
HEADER TRANSCRIPTION/DNA 12-MAY-95 1RCS TITLE NMR STUDY OF TRP REPRESSOR-OPERATOR DNA COMPLEX COMPND MOL_ID: 1; COMPND 2 MOLECULE: DNA (5'- COMPND 3 D(*CP*GP*TP*AP*CP*TP*AP*GP*TP*TP*AP*AP*CP*TP*AP*GP*TP*AP*CP*G)-3'); COMPND 4 CHAIN: E, F; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: TRP REPRESSOR; COMPND 8 CHAIN: A, B SOURCE MOL_ID: 1; SOURCE 2 SYNTHETIC: YES; SOURCE 3 MOL_ID: 2; SOURCE 4 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI; SOURCE 5 ORGANISM_TAXID: 562; SOURCE 6 STRAIN: CY15070 AND CY17071 KEYWDS TRANSCRIPTION REGULATION, REPRESSOR, DNA-BINDING, TRP, DNA, KEYWDS 2 TRANSCRIPTION-DNA COMPLEX EXPDTA SOLUTION NMR NUMMDL 15 AUTHOR D.ZHAO,Z.ZHENG REVDAT 3 02-MAR-22 1RCS 1 REMARK REVDAT 2 24-FEB-09 1RCS 1 VERSN REVDAT 1 20-JUN-96 1RCS 0 JRNL AUTH H.ZHANG,D.ZHAO,M.REVINGTON,W.LEE,X.JIA,C.ARROWSMITH, JRNL AUTH 2 O.JARDETZKY JRNL TITL THE SOLUTION STRUCTURES OF THE TRP REPRESSOR-OPERATOR DNA JRNL TITL 2 COMPLEX. JRNL REF J.MOL.BIOL. V. 238 592 1994 JRNL REFN ISSN 0022-2836 JRNL PMID 8176748 JRNL DOI 10.1006/JMBI.1994.1317 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH D.ZHAO,C.H.ARROWSMITH,X.JIA,O.JARDETZKY REMARK 1 TITL REFINED SOLUTION STRUCTURES OF THE ESCHERICHIA COLI TRP REMARK 1 TITL 2 HOLO-AND APOREPRESSOR REMARK 1 REF J.MOL.BIOL. V. 229 735 1993 REMARK 1 REFN ISSN 0022-2836 REMARK 1 REFERENCE 2 REMARK 1 AUTH D.ZHAO,O.JARDETZKY REMARK 1 TITL SEQUENTIAL SIMULATED ANNEALING: AN EFFICIENT PROCEDURE FOR REMARK 1 TITL 2 STRUCTURAL REFINEMENT BASED ON NMR CONSTRAINTS REMARK 1 REF J.PHYS.CHEM. V. 97 3007 1993 REMARK 1 REFN ISSN 0022-3654 REMARK 1 REFERENCE 3 REMARK 1 AUTH C.ARROWSMITH,R.PACHTER,R.ALTMAN,O.JARDETZKY REMARK 1 TITL THE SOLUTION STRUCTURES OF ESCHERICHIA COLI TRP REPRESSOR REMARK 1 TITL 2 AND TRP APOREPRESSOR AT AN INTERMEDIATE RESOLUTION REMARK 1 REF EUR.J.BIOCHEM. V. 202 53 1991 REMARK 1 REFN ISSN 0014-2956 REMARK 1 REFERENCE 4 REMARK 1 AUTH C.H.ARROWSMITH,R.PACHTER,R.B.ALTMAN,S.B.IYER,O.JARDETZKY REMARK 1 TITL SEQUENCE-SPECIFIC 1H NMR ASSIGNMENTS AND SECONDARY STRUCTURE REMARK 1 TITL 2 IN SOLUTION OF ESCHERICHIA COLI TRP REPRESSOR REMARK 1 REF BIOCHEMISTRY V. 29 6332 1990 REMARK 1 REFN ISSN 0006-2960 REMARK 1 REFERENCE 5 REMARK 1 AUTH C.H.ARROWSMITH,J.CAREY,L.TREAT-CLEMONS,O.JARDETZKY REMARK 1 TITL NMR ASSIGNMENTS FOR THE AMINO-TERMINAL RESIDUES OF TRP REMARK 1 TITL 2 REPRESSOR AND THEIR ROLE IN DNA BINDING REMARK 1 REF BIOCHEMISTRY V. 28 3875 1989 REMARK 1 REFN ISSN 0006-2960 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1RCS 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_1000176024. 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 : 15 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: TETRAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, A, B 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 1-15 REMARK 465 RES C SSSEQI REMARK 465 ASP A 108 REMARK 465 ASP B 608 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS 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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) 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 RES CSSEQI ATM2 DEVIATION REMARK 500 1 DC E 1 C4' DC E 1 C3' -0.067 REMARK 500 1 DC E 1 C3' DC E 1 C2' -0.104 REMARK 500 1 DC E 1 C2' DC E 1 C1' 0.067 REMARK 500 1 DC E 1 O4' DC E 1 C1' 0.114 REMARK 500 1 DC E 1 O3' DC E 1 C3' 0.123 REMARK 500 1 DG E 2 C5' DG E 2 C4' 0.056 REMARK 500 1 DG E 2 C3' DG E 2 C2' -0.101 REMARK 500 1 DG E 2 C2' DG E 2 C1' 0.064 REMARK 500 1 DG E 2 O4' DG E 2 C1' 0.111 REMARK 500 1 DG E 2 O3' DG E 2 C3' 0.123 REMARK 500 1 DT E 3 C5' DT E 3 C4' 0.050 REMARK 500 1 DT E 3 C3' DT E 3 C2' -0.103 REMARK 500 1 DT E 3 C2' DT E 3 C1' 0.074 REMARK 500 1 DT E 3 O4' DT E 3 C1' 0.114 REMARK 500 1 DT E 3 O3' DT E 3 C3' 0.123 REMARK 500 1 DT E 3 N1 DT E 3 C2 0.058 REMARK 500 1 DT E 3 C5 DT E 3 C7 0.047 REMARK 500 1 DA E 4 C3' DA E 4 C2' -0.098 REMARK 500 1 DA E 4 C2' DA E 4 C1' 0.066 REMARK 500 1 DA E 4 O4' DA E 4 C1' 0.110 REMARK 500 1 DA E 4 O3' DA E 4 C3' 0.130 REMARK 500 1 DC E 5 C5' DC E 5 C4' 0.047 REMARK 500 1 DC E 5 C3' DC E 5 C2' -0.116 REMARK 500 1 DC E 5 C2' DC E 5 C1' 0.082 REMARK 500 1 DC E 5 O4' DC E 5 C1' 0.106 REMARK 500 1 DC E 5 O3' DC E 5 C3' 0.100 REMARK 500 1 DT E 6 C3' DT E 6 C2' -0.101 REMARK 500 1 DT E 6 C2' DT E 6 C1' 0.069 REMARK 500 1 DT E 6 O4' DT E 6 C1' 0.111 REMARK 500 1 DT E 6 O3' DT E 6 C3' 0.130 REMARK 500 1 DT E 6 N1 DT E 6 C2 0.060 REMARK 500 1 DT E 6 C5 DT E 6 C7 0.043 REMARK 500 1 DA E 7 C4' DA E 7 C3' -0.069 REMARK 500 1 DA E 7 C3' DA E 7 C2' -0.103 REMARK 500 1 DA E 7 O4' DA E 7 C1' 0.071 REMARK 500 1 DA E 7 O3' DA E 7 C3' 0.111 REMARK 500 1 DA E 7 N7 DA E 7 C8 -0.043 REMARK 500 1 DG E 8 C4' DG E 8 C3' -0.066 REMARK 500 1 DG E 8 C3' DG E 8 C2' -0.095 REMARK 500 1 DG E 8 O4' DG E 8 C1' 0.112 REMARK 500 1 DG E 8 O3' DG E 8 C3' 0.107 REMARK 500 1 DT E 9 C5' DT E 9 C4' 0.047 REMARK 500 1 DT E 9 C4' DT E 9 C3' -0.066 REMARK 500 1 DT E 9 C3' DT E 9 C2' -0.107 REMARK 500 1 DT E 9 C2' DT E 9 C1' 0.071 REMARK 500 1 DT E 9 O4' DT E 9 C1' 0.120 REMARK 500 1 DT E 9 O3' DT E 9 C3' 0.122 REMARK 500 1 DT E 9 N1 DT E 9 C2 0.066 REMARK 500 1 DT E 9 C5 DT E 9 C7 0.048 REMARK 500 1 DT E 10 C4' DT E 10 C3' -0.061 REMARK 500 REMARK 500 THIS ENTRY HAS 3104 BOND DEVIATIONS. 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 DC E 1 C4' - C3' - C2' ANGL. DEV. = 13.6 DEGREES REMARK 500 1 DC E 1 O4' - C1' - N1 ANGL. DEV. = 10.6 DEGREES REMARK 500 1 DC E 1 N1 - C2 - O2 ANGL. DEV. = 3.9 DEGREES REMARK 500 1 DC E 1 C3' - O3' - P ANGL. DEV. = 8.1 DEGREES REMARK 500 1 DG E 2 C4' - C3' - C2' ANGL. DEV. = 13.9 DEGREES REMARK 500 1 DG E 2 O4' - C1' - N9 ANGL. DEV. = 11.4 DEGREES REMARK 500 1 DG E 2 C5 - N7 - C8 ANGL. DEV. = -4.2 DEGREES REMARK 500 1 DG E 2 N7 - C8 - N9 ANGL. DEV. = 7.4 DEGREES REMARK 500 1 DG E 2 C8 - N9 - C4 ANGL. DEV. = -4.4 DEGREES REMARK 500 1 DG E 2 C3' - O3' - P ANGL. DEV. = 8.6 DEGREES REMARK 500 1 DT E 3 C4' - C3' - C2' ANGL. DEV. = 13.8 DEGREES REMARK 500 1 DT E 3 O4' - C1' - N1 ANGL. DEV. = 9.2 DEGREES REMARK 500 1 DT E 3 C6 - C5 - C7 ANGL. DEV. = -4.0 DEGREES REMARK 500 1 DT E 3 C3' - O3' - P ANGL. DEV. = 8.2 DEGREES REMARK 500 1 DA E 4 C4' - C3' - C2' ANGL. DEV. = 13.8 DEGREES REMARK 500 1 DA E 4 O4' - C1' - N9 ANGL. DEV. = 10.7 DEGREES REMARK 500 1 DA E 4 C5 - N7 - C8 ANGL. DEV. = -3.9 DEGREES REMARK 500 1 DA E 4 N7 - C8 - N9 ANGL. DEV. = 6.5 DEGREES REMARK 500 1 DA E 4 C8 - N9 - C4 ANGL. DEV. = -4.0 DEGREES REMARK 500 1 DA E 4 C3' - O3' - P ANGL. DEV. = 9.0 DEGREES REMARK 500 1 DC E 5 C2' - C3' - O3' ANGL. DEV. = -15.6 DEGREES REMARK 500 1 DC E 5 C4' - C3' - C2' ANGL. DEV. = 12.6 DEGREES REMARK 500 1 DC E 5 O4' - C1' - N1 ANGL. DEV. = 12.1 DEGREES REMARK 500 1 DC E 5 N1 - C2 - O2 ANGL. DEV. = 3.8 DEGREES REMARK 500 1 DT E 6 C4' - C3' - C2' ANGL. DEV. = 13.6 DEGREES REMARK 500 1 DT E 6 N1 - C1' - C2' ANGL. DEV. = 8.5 DEGREES REMARK 500 1 DT E 6 O4' - C1' - N1 ANGL. DEV. = 11.8 DEGREES REMARK 500 1 DT E 6 C3' - O3' - P ANGL. DEV. = 8.6 DEGREES REMARK 500 1 DA E 7 C4' - C3' - C2' ANGL. DEV. = 9.9 DEGREES REMARK 500 1 DA E 7 N9 - C1' - C2' ANGL. DEV. = 18.7 DEGREES REMARK 500 1 DA E 7 C5 - N7 - C8 ANGL. DEV. = -3.5 DEGREES REMARK 500 1 DA E 7 N7 - C8 - N9 ANGL. DEV. = 7.5 DEGREES REMARK 500 1 DA E 7 C8 - N9 - C4 ANGL. DEV. = -4.4 DEGREES REMARK 500 1 DG E 8 C4' - C3' - C2' ANGL. DEV. = 12.3 DEGREES REMARK 500 1 DG E 8 O4' - C1' - N9 ANGL. DEV. = 11.4 DEGREES REMARK 500 1 DG E 8 C5 - N7 - C8 ANGL. DEV. = -3.7 DEGREES REMARK 500 1 DG E 8 N7 - C8 - N9 ANGL. DEV. = 7.1 DEGREES REMARK 500 1 DG E 8 C8 - N9 - C4 ANGL. DEV. = -4.4 DEGREES REMARK 500 1 DT E 9 C4' - C3' - C2' ANGL. DEV. = 14.2 DEGREES REMARK 500 1 DT E 9 O4' - C1' - N1 ANGL. DEV. = 10.6 DEGREES REMARK 500 1 DT E 9 C6 - C5 - C7 ANGL. DEV. = -4.3 DEGREES REMARK 500 1 DT E 9 C3' - O3' - P ANGL. DEV. = 9.1 DEGREES REMARK 500 1 DT E 10 C4' - C3' - C2' ANGL. DEV. = 13.3 DEGREES REMARK 500 1 DT E 10 O4' - C1' - N1 ANGL. DEV. = 10.8 DEGREES REMARK 500 1 DT E 10 C6 - C5 - C7 ANGL. DEV. = -4.2 DEGREES REMARK 500 1 DT E 10 C3' - O3' - P ANGL. DEV. = 8.5 DEGREES REMARK 500 1 DA E 11 C4' - C3' - C2' ANGL. DEV. = 12.1 DEGREES REMARK 500 1 DA E 11 O4' - C1' - N9 ANGL. DEV. = 12.7 DEGREES REMARK 500 1 DA E 11 C5 - N7 - C8 ANGL. DEV. = -3.4 DEGREES REMARK 500 1 DA E 11 N7 - C8 - N9 ANGL. DEV. = 6.6 DEGREES REMARK 500 REMARK 500 THIS ENTRY HAS 2715 ANGLE DEVIATIONS. 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 SER A 8 125.79 66.56 REMARK 500 1 ALA A 10 122.49 63.18 REMARK 500 1 ALA A 12 -50.77 -145.05 REMARK 500 1 GLU A 13 124.80 65.57 REMARK 500 1 GLN A 17 77.72 -113.58 REMARK 500 1 GLU A 18 -68.74 -149.90 REMARK 500 1 ASN A 32 -88.70 -88.28 REMARK 500 1 ASP A 33 48.46 152.90 REMARK 500 1 LEU A 43 -68.25 -135.16 REMARK 500 1 THR A 44 160.59 121.47 REMARK 500 1 GLU A 65 -59.40 -138.41 REMARK 500 1 LEU A 75 -44.94 -132.98 REMARK 500 1 LYS A 106 -64.55 -91.71 REMARK 500 1 ALA B 509 -48.43 -159.05 REMARK 500 1 MET B 511 -71.64 79.23 REMARK 500 1 GLU B 518 -82.37 -119.38 REMARK 500 1 TRP B 519 -29.32 -36.74 REMARK 500 1 ASN B 532 -91.85 -90.54 REMARK 500 1 ASP B 533 54.47 155.10 REMARK 500 1 LEU B 543 -106.97 -119.09 REMARK 500 1 THR B 544 165.78 179.13 REMARK 500 1 GLN B 568 -84.66 -98.03 REMARK 500 1 LEU B 575 -64.64 -93.81 REMARK 500 1 LEU B 604 -61.12 -104.88 REMARK 500 1 LYS B 606 96.72 66.69 REMARK 500 2 GLU A 18 -70.27 -149.24 REMARK 500 2 ASN A 32 -83.21 -92.63 REMARK 500 2 ASP A 33 44.16 145.51 REMARK 500 2 LEU A 41 -50.08 -125.57 REMARK 500 2 LEU A 43 -83.38 -110.88 REMARK 500 2 THR A 44 166.09 150.52 REMARK 500 2 LEU A 75 -40.56 -138.16 REMARK 500 2 LYS A 106 -45.86 91.87 REMARK 500 2 SER B 505 102.48 63.57 REMARK 500 2 ALA B 510 159.23 68.21 REMARK 500 2 ALA B 512 -43.65 -155.54 REMARK 500 2 GLU B 518 -84.35 -122.28 REMARK 500 2 ASN B 532 -90.01 -89.63 REMARK 500 2 ASP B 533 48.90 155.56 REMARK 500 2 LEU B 543 -98.85 -134.34 REMARK 500 2 THR B 544 175.11 158.17 REMARK 500 2 GLU B 547 -76.23 -45.71 REMARK 500 2 GLU B 565 -52.69 -162.51 REMARK 500 2 LEU B 575 -43.86 -135.97 REMARK 500 3 ALA A 10 -51.94 -156.23 REMARK 500 3 ARG A 15 119.14 61.83 REMARK 500 3 HIS A 16 103.67 56.34 REMARK 500 3 GLN A 17 63.59 -111.46 REMARK 500 3 GLU A 18 -92.46 -132.08 REMARK 500 3 ASN A 32 -90.61 -90.94 REMARK 500 REMARK 500 THIS ENTRY HAS 360 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 DC E 13 0.07 SIDE CHAIN REMARK 500 1 DG E 16 0.07 SIDE CHAIN REMARK 500 1 DA F 4 0.05 SIDE CHAIN REMARK 500 1 DC F 13 0.06 SIDE CHAIN REMARK 500 1 DG F 16 0.08 SIDE CHAIN REMARK 500 1 ARG A 69 0.11 SIDE CHAIN REMARK 500 1 ARG B 554 0.15 SIDE CHAIN REMARK 500 1 ARG B 569 0.19 SIDE CHAIN REMARK 500 2 DA E 7 0.06 SIDE CHAIN REMARK 500 2 DG E 16 0.08 SIDE CHAIN REMARK 500 2 DA F 4 0.06 SIDE CHAIN REMARK 500 2 DG F 16 0.08 SIDE CHAIN REMARK 500 2 ARG A 48 0.08 SIDE CHAIN REMARK 500 2 ARG A 54 0.09 SIDE CHAIN REMARK 500 2 ARG A 56 0.09 SIDE CHAIN REMARK 500 2 ARG A 63 0.09 SIDE CHAIN REMARK 500 2 ARG A 69 0.07 SIDE CHAIN REMARK 500 2 ARG B 597 0.08 SIDE CHAIN REMARK 500 3 DA E 4 0.08 SIDE CHAIN REMARK 500 3 DG E 16 0.07 SIDE CHAIN REMARK 500 3 DA F 4 0.07 SIDE CHAIN REMARK 500 3 DC F 13 0.07 SIDE CHAIN REMARK 500 3 DG F 16 0.07 SIDE CHAIN REMARK 500 3 ARG A 21 0.08 SIDE CHAIN REMARK 500 3 ARG A 56 0.10 SIDE CHAIN REMARK 500 3 ARG A 69 0.11 SIDE CHAIN REMARK 500 3 ARG B 548 0.09 SIDE CHAIN REMARK 500 3 ARG B 563 0.14 SIDE CHAIN REMARK 500 3 ARG B 569 0.17 SIDE CHAIN REMARK 500 4 DG E 16 0.06 SIDE CHAIN REMARK 500 4 DA F 4 0.05 SIDE CHAIN REMARK 500 4 DG F 16 0.07 SIDE CHAIN REMARK 500 4 ARG A 54 0.11 SIDE CHAIN REMARK 500 4 ARG A 69 0.11 SIDE CHAIN REMARK 500 4 ARG B 563 0.08 SIDE CHAIN REMARK 500 5 DA E 4 0.06 SIDE CHAIN REMARK 500 5 DA E 7 0.05 SIDE CHAIN REMARK 500 5 DG E 16 0.06 SIDE CHAIN REMARK 500 5 DC F 13 0.06 SIDE CHAIN REMARK 500 5 DG F 16 0.07 SIDE CHAIN REMARK 500 5 ARG A 63 0.08 SIDE CHAIN REMARK 500 5 ARG A 69 0.12 SIDE CHAIN REMARK 500 5 ARG B 554 0.09 SIDE CHAIN REMARK 500 5 ARG B 563 0.10 SIDE CHAIN REMARK 500 5 ARG B 569 0.20 SIDE CHAIN REMARK 500 6 DA E 4 0.07 SIDE CHAIN REMARK 500 6 DG E 16 0.07 SIDE CHAIN REMARK 500 6 DA F 7 0.06 SIDE CHAIN REMARK 500 6 DG F 16 0.09 SIDE CHAIN REMARK 500 6 ARG A 63 0.10 SIDE CHAIN REMARK 500 REMARK 500 THIS ENTRY HAS 127 PLANE DEVIATIONS. REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRP A 898 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRP B 998 DBREF 1RCS A 4 107 UNP P0A881 TRPR_ECOLI 3 106 DBREF 1RCS B 504 607 UNP P0A881 TRPR_ECOLI 3 106 DBREF 1RCS E 1 20 PDB 1RCS 1RCS 1 20 DBREF 1RCS F 1 20 PDB 1RCS 1RCS 1 20 SEQRES 1 E 20 DC DG DT DA DC DT DA DG DT DT DA DA DC SEQRES 2 E 20 DT DA DG DT DA DC DG SEQRES 1 F 20 DC DG DT DA DC DT DA DG DT DT DA DA DC SEQRES 2 F 20 DT DA DG DT DA DC DG SEQRES 1 A 105 GLN SER PRO TYR SER ALA ALA MET ALA GLU GLN ARG HIS SEQRES 2 A 105 GLN GLU TRP LEU ARG PHE VAL ASP LEU LEU LYS ASN ALA SEQRES 3 A 105 TYR GLN ASN ASP LEU HIS LEU PRO LEU LEU ASN LEU MET SEQRES 4 A 105 LEU THR PRO ASP GLU ARG GLU ALA LEU GLY THR ARG VAL SEQRES 5 A 105 ARG ILE VAL GLU GLU LEU LEU ARG GLY GLU MET SER GLN SEQRES 6 A 105 ARG GLU LEU LYS ASN GLU LEU GLY ALA GLY ILE ALA THR SEQRES 7 A 105 ILE THR ARG GLY SER ASN SER LEU LYS ALA ALA PRO VAL SEQRES 8 A 105 GLU LEU ARG GLN TRP LEU GLU GLU VAL LEU LEU LYS SER SEQRES 9 A 105 ASP SEQRES 1 B 105 GLN SER PRO TYR SER ALA ALA MET ALA GLU GLN ARG HIS SEQRES 2 B 105 GLN GLU TRP LEU ARG PHE VAL ASP LEU LEU LYS ASN ALA SEQRES 3 B 105 TYR GLN ASN ASP LEU HIS LEU PRO LEU LEU ASN LEU MET SEQRES 4 B 105 LEU THR PRO ASP GLU ARG GLU ALA LEU GLY THR ARG VAL SEQRES 5 B 105 ARG ILE VAL GLU GLU LEU LEU ARG GLY GLU MET SER GLN SEQRES 6 B 105 ARG GLU LEU LYS ASN GLU LEU GLY ALA GLY ILE ALA THR SEQRES 7 B 105 ILE THR ARG GLY SER ASN SER LEU LYS ALA ALA PRO VAL SEQRES 8 B 105 GLU LEU ARG GLN TRP LEU GLU GLU VAL LEU LEU LYS SER SEQRES 9 B 105 ASP HET TRP A 898 27 HET TRP B 998 27 HETNAM TRP TRYPTOPHAN FORMUL 5 TRP 2(C11 H12 N2 O2) HELIX 1 1 TRP A 19 GLN A 31 1 13 HELIX 2 2 HIS A 35 LEU A 41 1 7 HELIX 3 3 PRO A 45 LEU A 61 1 17 HELIX 4 4 LEU A 71 GLU A 74 1 4 HELIX 5 5 ILE A 79 LEU A 89 1 11 HELIX 6 6 ARG A 97 VAL A 103 1 7 HELIX 7 7 TRP B 519 GLN B 531 1 13 HELIX 8 8 LEU B 539 MET B 542 1 4 HELIX 9 9 PRO B 545 LEU B 561 1 17 HELIX 10 10 ILE B 579 LEU B 589 1 11 HELIX 11 11 ARG B 597 LEU B 604 1 8 SITE 1 AC1 7 ILE A 57 THR A 81 ARG A 84 GLY A 85 SITE 2 AC1 7 SER A 88 LEU B 543 THR B 544 SITE 1 AC2 7 THR A 44 ILE B 557 THR B 581 ARG B 584 SITE 2 AC2 7 GLY B 585 SER B 588 DC F 13 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