Header list of 1co0.pdb file
Complete list - b 16 2 Bytes
HEADER TRANSCRIPTION 30-MAY-99 1CO0
TITLE NMR STUDY OF TRP REPRESSOR-MTR OPERATOR DNA COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 5'-D(*TP*GP*TP*AP*CP*TP*CP*GP*TP*GP*TP*AP*CP*TP*GP*GP*TP*AP
COMPND 3 *CP*A)-3';
COMPND 4 CHAIN: E;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: 5'-D(*TP*GP*TP*AP*CP*CP*AP*GP*TP*AP*CP*AP*CP*GP*AP*GP*TP*AP
COMPND 8 *CP*A)-3';
COMPND 9 CHAIN: F;
COMPND 10 ENGINEERED: YES;
COMPND 11 MOL_ID: 3;
COMPND 12 MOLECULE: TRP OPERON REPRESSOR;
COMPND 13 CHAIN: A, B;
COMPND 14 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: TRP OPERON SEQUENCE FROM ESCHERICHIA COLI;
SOURCE 4 MOL_ID: 2;
SOURCE 5 SYNTHETIC: YES;
SOURCE 6 OTHER_DETAILS: TRP OPERON SEQUENCE FROM ESCHERICHIA COLI;
SOURCE 7 MOL_ID: 3;
SOURCE 8 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 9 ORGANISM_TAXID: 562;
SOURCE 10 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 11 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 12 EXPRESSION_SYSTEM_STRAIN: CY15070,CY17071
KEYWDS TRANSCRIPTION REGULATION, REPRESSOR, DNA-BINDING, TRP, DNA,
KEYWDS 2 TRANSCRIPTION
EXPDTA SOLUTION NMR
NUMMDL 15
AUTHOR G.P.ZHOU,L.BROCCHIERI,O.JARDETZKY
REVDAT 3 16-FEB-22 1CO0 1 REMARK
REVDAT 2 24-FEB-09 1CO0 1 VERSN
REVDAT 1 16-SEP-03 1CO0 0
JRNL AUTH L.BROCCHIERI,G.P.ZHOU,O.JARDETZKY
JRNL TITL ALLOSTERY AND INDUCED FIT, NMR AND MOLECULAR MODELING STUDY
JRNL TITL 2 OF THE TRP-REPRESSOR - MTR DNA COMPLEX
JRNL EDIT G.R.EATON, G.P.ZHOU, O.JARDETZKY
JRNL REF STRUCTURES AND MECHANISMS, V. 827 340 2002
JRNL REF 2 ACS SYMPOSIUM SERIES
JRNL REFN ISSN 0841-2373
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH H.ZHANG,D.ZHAO,M.REVINGTON,W.LEE,X.JIA,C.ARROWSMITH,
REMARK 1 AUTH 2 O.JARDETZKY
REMARK 1 TITL THE SOLUTION STRUCTURES OF THE TRP REPRESSOR-OPERATOR DNA
REMARK 1 TITL 2 COMPLEX
REMARK 1 REF J.MOL.BIOL. V. 238 592 1994
REMARK 1 REFN ISSN 0022-2836
REMARK 1 DOI 10.1006/JMBI.1994.1317
REMARK 1 REFERENCE 2
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 DOI 10.1006/JMBI.1993.1076
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1CO0 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-JUN-99.
REMARK 100 THE DEPOSITION ID IS D_1000001131.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : 5.7
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 : X-PLOR
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 30
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION
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 ALA A 2
REMARK 465 GLN A 3
REMARK 465 ALA B 2
REMARK 465 GLN B 3
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 O GLY A 78 H ILE A 82 0.90
REMARK 500 HG3 LYS A 90 H ALA A 91 1.28
REMARK 500 O PRO B 93 H ARG B 97 1.33
REMARK 500 O ALA A 77 HG1 THR A 81 1.39
REMARK 500 O GLY B 78 H ILE B 82 1.40
REMARK 500 O ASN A 87 H LYS A 90 1.41
REMARK 500 O THR A 81 H GLY A 85 1.42
REMARK 500 O GLU B 101 H LEU B 105 1.52
REMARK 500 O ARG B 97 H GLU B 101 1.53
REMARK 500 O ARG B 54 HG13 ILE B 57 1.53
REMARK 500 O ARG B 84 H ASN B 87 1.54
REMARK 500 O GLY B 85 H SER B 88 1.54
REMARK 500 O VAL A 55 H GLU A 59 1.56
REMARK 500 O LEU A 26 H TYR A 30 1.56
REMARK 500 O ALA A 50 H ARG A 54 1.56
REMARK 500 O LEU A 43 HH11 ARG B 54 1.58
REMARK 500 O PRO A 45 H ARG A 48 1.59
REMARK 500 O GLY A 78 N ILE A 82 1.76
REMARK 500 O ALA A 77 OG1 THR A 81 1.96
REMARK 500 O LEU B 36 OD1 ASN B 40 2.11
REMARK 500 OP2 DA F 4 OG1 THR A 83 2.14
REMARK 500 O GLY B 78 N ILE B 82 2.16
REMARK 500
REMARK 500 REMARK: NULL
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 DT E 1 C3' DT E 1 C2' -0.098
REMARK 500 1 DT E 1 C2' DT E 1 C1' -0.086
REMARK 500 1 DG E 2 C3' DG E 2 C2' -0.097
REMARK 500 1 DG E 2 C2' DG E 2 C1' -0.087
REMARK 500 1 DT E 3 C3' DT E 3 C2' -0.098
REMARK 500 1 DT E 3 C2' DT E 3 C1' -0.087
REMARK 500 1 DA E 4 C3' DA E 4 C2' -0.096
REMARK 500 1 DA E 4 C2' DA E 4 C1' -0.086
REMARK 500 1 DC E 5 C3' DC E 5 C2' -0.098
REMARK 500 1 DC E 5 C2' DC E 5 C1' -0.086
REMARK 500 1 DT E 6 C3' DT E 6 C2' -0.098
REMARK 500 1 DT E 6 C2' DT E 6 C1' -0.088
REMARK 500 1 DC E 7 C3' DC E 7 C2' -0.097
REMARK 500 1 DC E 7 C2' DC E 7 C1' -0.086
REMARK 500 1 DG E 8 C3' DG E 8 C2' -0.096
REMARK 500 1 DG E 8 C2' DG E 8 C1' -0.089
REMARK 500 1 DT E 9 C3' DT E 9 C2' -0.097
REMARK 500 1 DT E 9 C2' DT E 9 C1' -0.087
REMARK 500 1 DG E 10 C3' DG E 10 C2' -0.098
REMARK 500 1 DG E 10 C2' DG E 10 C1' -0.088
REMARK 500 1 DT E 11 C3' DT E 11 C2' -0.097
REMARK 500 1 DT E 11 C2' DT E 11 C1' -0.082
REMARK 500 1 DA E 12 C3' DA E 12 C2' -0.111
REMARK 500 1 DA E 12 C2' DA E 12 C1' -0.094
REMARK 500 1 DC E 13 C3' DC E 13 C2' -0.100
REMARK 500 1 DC E 13 C2' DC E 13 C1' -0.089
REMARK 500 1 DT E 14 C3' DT E 14 C2' -0.089
REMARK 500 1 DT E 14 C2' DT E 14 C1' -0.085
REMARK 500 1 DG E 15 C3' DG E 15 C2' -0.092
REMARK 500 1 DG E 15 C2' DG E 15 C1' -0.095
REMARK 500 1 DG E 16 C3' DG E 16 C2' -0.097
REMARK 500 1 DG E 16 C2' DG E 16 C1' -0.093
REMARK 500 1 DT E 17 C3' DT E 17 C2' -0.097
REMARK 500 1 DT E 17 C2' DT E 17 C1' -0.089
REMARK 500 1 DA E 18 C3' DA E 18 C2' -0.095
REMARK 500 1 DA E 18 C2' DA E 18 C1' -0.087
REMARK 500 1 DC E 19 C3' DC E 19 C2' -0.097
REMARK 500 1 DC E 19 C2' DC E 19 C1' -0.085
REMARK 500 1 DA E 20 C3' DA E 20 C2' -0.098
REMARK 500 1 DA E 20 C2' DA E 20 C1' -0.086
REMARK 500 1 DT F 1 C3' DT F 1 C2' -0.097
REMARK 500 1 DT F 1 C2' DT F 1 C1' -0.085
REMARK 500 1 DG F 2 C3' DG F 2 C2' -0.092
REMARK 500 1 DG F 2 C2' DG F 2 C1' -0.089
REMARK 500 1 DT F 3 C3' DT F 3 C2' -0.085
REMARK 500 1 DT F 3 C2' DT F 3 C1' -0.101
REMARK 500 1 DA F 4 C3' DA F 4 C2' -0.098
REMARK 500 1 DA F 4 C2' DA F 4 C1' -0.090
REMARK 500 1 DC F 5 C3' DC F 5 C2' -0.098
REMARK 500 1 DC F 5 C2' DC F 5 C1' -0.090
REMARK 500
REMARK 500 THIS ENTRY HAS 1200 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 DT E 1 C3' - C2' - C1' ANGL. DEV. = 12.9 DEGREES
REMARK 500 1 DT E 1 O4' - C1' - N1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 1 DG E 2 C3' - C2' - C1' ANGL. DEV. = 13.0 DEGREES
REMARK 500 1 DG E 2 O4' - C1' - N9 ANGL. DEV. = 3.1 DEGREES
REMARK 500 1 DG E 2 N7 - C8 - N9 ANGL. DEV. = 4.5 DEGREES
REMARK 500 1 DG E 2 C8 - N9 - C4 ANGL. DEV. = -2.6 DEGREES
REMARK 500 1 DT E 3 C3' - C2' - C1' ANGL. DEV. = 12.9 DEGREES
REMARK 500 1 DT E 3 O4' - C1' - N1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 1 DA E 4 C3' - C2' - C1' ANGL. DEV. = 13.0 DEGREES
REMARK 500 1 DA E 4 O4' - C1' - N9 ANGL. DEV. = 2.8 DEGREES
REMARK 500 1 DA E 4 N7 - C8 - N9 ANGL. DEV. = 3.7 DEGREES
REMARK 500 1 DC E 5 C3' - C2' - C1' ANGL. DEV. = 13.0 DEGREES
REMARK 500 1 DC E 5 O4' - C1' - N1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 1 DT E 6 C3' - C2' - C1' ANGL. DEV. = 13.0 DEGREES
REMARK 500 1 DT E 6 O4' - C1' - N1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 1 DC E 7 C3' - C2' - C1' ANGL. DEV. = 12.8 DEGREES
REMARK 500 1 DC E 7 O4' - C1' - N1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 1 DG E 8 C3' - C2' - C1' ANGL. DEV. = 13.0 DEGREES
REMARK 500 1 DG E 8 O4' - C1' - N9 ANGL. DEV. = 3.1 DEGREES
REMARK 500 1 DG E 8 N7 - C8 - N9 ANGL. DEV. = 4.6 DEGREES
REMARK 500 1 DG E 8 C8 - N9 - C4 ANGL. DEV. = -2.6 DEGREES
REMARK 500 1 DT E 9 C3' - C2' - C1' ANGL. DEV. = 12.9 DEGREES
REMARK 500 1 DT E 9 O4' - C1' - N1 ANGL. DEV. = 2.9 DEGREES
REMARK 500 1 DG E 10 C3' - C2' - C1' ANGL. DEV. = 13.0 DEGREES
REMARK 500 1 DG E 10 O4' - C1' - N9 ANGL. DEV. = 3.2 DEGREES
REMARK 500 1 DG E 10 N7 - C8 - N9 ANGL. DEV. = 4.5 DEGREES
REMARK 500 1 DG E 10 C8 - N9 - C4 ANGL. DEV. = -2.6 DEGREES
REMARK 500 1 DT E 11 C3' - C2' - C1' ANGL. DEV. = 12.9 DEGREES
REMARK 500 1 DT E 11 O4' - C1' - N1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 1 DA E 12 C3' - C2' - C1' ANGL. DEV. = 13.0 DEGREES
REMARK 500 1 DA E 12 O4' - C1' - N9 ANGL. DEV. = 2.8 DEGREES
REMARK 500 1 DA E 12 N7 - C8 - N9 ANGL. DEV. = 3.8 DEGREES
REMARK 500 1 DC E 13 C3' - C2' - C1' ANGL. DEV. = 12.7 DEGREES
REMARK 500 1 DC E 13 O4' - C1' - N1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 1 DT E 14 C3' - C2' - C1' ANGL. DEV. = 12.2 DEGREES
REMARK 500 1 DT E 14 O4' - C1' - N1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 1 DG E 15 C3' - C2' - C1' ANGL. DEV. = 11.4 DEGREES
REMARK 500 1 DG E 15 O4' - C1' - N9 ANGL. DEV. = 4.8 DEGREES
REMARK 500 1 DG E 15 C5 - N7 - C8 ANGL. DEV. = -3.3 DEGREES
REMARK 500 1 DG E 15 N7 - C8 - N9 ANGL. DEV. = 4.3 DEGREES
REMARK 500 1 DG E 15 C8 - N9 - C4 ANGL. DEV. = -2.6 DEGREES
REMARK 500 1 DG E 16 C3' - C2' - C1' ANGL. DEV. = 12.6 DEGREES
REMARK 500 1 DG E 16 O4' - C1' - N9 ANGL. DEV. = 3.2 DEGREES
REMARK 500 1 DG E 16 N7 - C8 - N9 ANGL. DEV. = 4.5 DEGREES
REMARK 500 1 DG E 16 C8 - N9 - C4 ANGL. DEV. = -2.7 DEGREES
REMARK 500 1 DT E 17 C3' - C2' - C1' ANGL. DEV. = 12.9 DEGREES
REMARK 500 1 DT E 17 O4' - C1' - N1 ANGL. DEV. = 2.9 DEGREES
REMARK 500 1 DA E 18 C3' - C2' - C1' ANGL. DEV. = 12.8 DEGREES
REMARK 500 1 DA E 18 O4' - C1' - N9 ANGL. DEV. = 2.2 DEGREES
REMARK 500 1 DA E 18 N7 - C8 - N9 ANGL. DEV. = 3.8 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 1683 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 TYR A 7 81.90 35.48
REMARK 500 1 MET A 11 -73.43 64.17
REMARK 500 1 ALA A 12 119.48 62.26
REMARK 500 1 GLU A 13 -148.37 35.15
REMARK 500 1 GLN A 14 36.63 -93.79
REMARK 500 1 ARG A 15 111.34 56.40
REMARK 500 1 LEU A 26 -73.71 -65.56
REMARK 500 1 ASN A 32 -138.57 -118.18
REMARK 500 1 LEU A 43 -88.42 -132.21
REMARK 500 1 GLU A 65 -157.99 174.55
REMARK 500 1 MET A 66 4.24 58.19
REMARK 500 1 GLN A 68 56.00 164.22
REMARK 500 1 ARG A 69 19.05 54.67
REMARK 500 1 GLU A 70 -25.70 -178.63
REMARK 500 1 ALA A 77 58.70 142.16
REMARK 500 1 ILE A 79 -82.49 -46.78
REMARK 500 1 LEU A 104 -44.39 -149.97
REMARK 500 1 LEU A 105 -31.45 -155.04
REMARK 500 1 SER A 107 -75.90 -177.80
REMARK 500 1 SER B 8 92.66 -61.60
REMARK 500 1 ALA B 9 -178.31 53.19
REMARK 500 1 ALA B 10 -77.61 -105.79
REMARK 500 1 MET B 11 -167.12 50.94
REMARK 500 1 ARG B 15 -65.79 65.72
REMARK 500 1 GLN B 17 -80.65 -61.26
REMARK 500 1 GLU B 18 46.67 26.48
REMARK 500 1 TRP B 19 -37.96 -145.19
REMARK 500 1 ASN B 32 -142.39 -118.79
REMARK 500 1 LEU B 34 34.14 -94.31
REMARK 500 1 ASN B 40 -53.43 -126.82
REMARK 500 1 LEU B 41 -7.99 -52.82
REMARK 500 1 LEU B 43 -74.74 63.45
REMARK 500 1 PRO B 45 16.41 -60.87
REMARK 500 1 ASP B 46 40.79 -74.53
REMARK 500 1 GLU B 47 18.19 -69.33
REMARK 500 1 ARG B 63 -56.98 -125.72
REMARK 500 1 SER B 67 159.53 59.80
REMARK 500 1 GLN B 68 73.50 34.18
REMARK 500 1 ARG B 69 -23.94 -171.32
REMARK 500 1 GLU B 70 -77.39 -110.11
REMARK 500 1 LEU B 71 30.04 179.37
REMARK 500 1 LEU B 75 29.84 -156.04
REMARK 500 1 ALA B 77 110.05 162.19
REMARK 500 1 ILE B 79 -45.67 -24.84
REMARK 500 1 ALA B 92 108.74 26.51
REMARK 500 1 VAL B 94 -35.73 -39.74
REMARK 500 1 LEU B 104 -51.17 -140.71
REMARK 500 1 LEU B 105 -55.59 -155.48
REMARK 500 1 LYS B 106 45.57 34.33
REMARK 500 2 SER A 5 88.93 -162.43
REMARK 500
REMARK 500 THIS ENTRY HAS 818 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 DT F 3 0.11 SIDE CHAIN
REMARK 500 1 ARG A 56 0.08 SIDE CHAIN
REMARK 500 2 DG E 15 0.05 SIDE CHAIN
REMARK 500 2 DA E 18 0.05 SIDE CHAIN
REMARK 500 2 DT F 3 0.06 SIDE CHAIN
REMARK 500 2 ARG A 54 0.09 SIDE CHAIN
REMARK 500 2 ARG A 84 0.09 SIDE CHAIN
REMARK 500 2 ARG B 54 0.12 SIDE CHAIN
REMARK 500 3 DT E 17 0.07 SIDE CHAIN
REMARK 500 3 DA E 18 0.07 SIDE CHAIN
REMARK 500 3 ARG A 21 0.19 SIDE CHAIN
REMARK 500 3 ARG A 54 0.08 SIDE CHAIN
REMARK 500 3 ARG A 56 0.08 SIDE CHAIN
REMARK 500 4 DG E 16 0.05 SIDE CHAIN
REMARK 500 4 DA E 18 0.05 SIDE CHAIN
REMARK 500 4 DT F 3 0.06 SIDE CHAIN
REMARK 500 4 DA F 4 0.05 SIDE CHAIN
REMARK 500 4 ARG A 54 0.12 SIDE CHAIN
REMARK 500 4 ARG B 21 0.08 SIDE CHAIN
REMARK 500 5 DG E 16 0.05 SIDE CHAIN
REMARK 500 5 DT F 3 0.10 SIDE CHAIN
REMARK 500 5 DA F 4 0.06 SIDE CHAIN
REMARK 500 5 ARG B 54 0.24 SIDE CHAIN
REMARK 500 6 DA E 18 0.07 SIDE CHAIN
REMARK 500 6 DT F 3 0.10 SIDE CHAIN
REMARK 500 6 ARG A 56 0.14 SIDE CHAIN
REMARK 500 7 DA E 18 0.06 SIDE CHAIN
REMARK 500 7 ARG A 54 0.08 SIDE CHAIN
REMARK 500 7 ARG A 56 0.11 SIDE CHAIN
REMARK 500 7 ARG B 21 0.09 SIDE CHAIN
REMARK 500 7 ARG B 54 0.13 SIDE CHAIN
REMARK 500 8 DA E 18 0.05 SIDE CHAIN
REMARK 500 8 DT F 3 0.07 SIDE CHAIN
REMARK 500 8 ARG A 56 0.08 SIDE CHAIN
REMARK 500 9 DA E 18 0.06 SIDE CHAIN
REMARK 500 9 DT F 3 0.07 SIDE CHAIN
REMARK 500 9 ARG A 84 0.09 SIDE CHAIN
REMARK 500 9 ARG B 54 0.20 SIDE CHAIN
REMARK 500 10 DA E 18 0.06 SIDE CHAIN
REMARK 500 10 DT F 3 0.08 SIDE CHAIN
REMARK 500 10 ARG A 84 0.14 SIDE CHAIN
REMARK 500 10 ARG B 54 0.10 SIDE CHAIN
REMARK 500 10 ARG B 97 0.29 SIDE CHAIN
REMARK 500 11 DA F 4 0.07 SIDE CHAIN
REMARK 500 12 DT F 3 0.06 SIDE CHAIN
REMARK 500 12 ARG B 84 0.10 SIDE CHAIN
REMARK 500 13 DT F 3 0.06 SIDE CHAIN
REMARK 500 13 ARG A 56 0.13 SIDE CHAIN
REMARK 500 13 ARG A 69 0.08 SIDE CHAIN
REMARK 500 14 DA E 18 0.05 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 56 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 B 109
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRP B 201
DBREF 1CO0 A 2 108 UNP P0A881 TRPR_ECOLI 1 107
DBREF 1CO0 B 2 108 UNP P0A881 TRPR_ECOLI 1 107
DBREF 1CO0 E 1 20 PDB 1CO0 1CO0 1 20
DBREF 1CO0 F 1 20 PDB 1CO0 1CO0 1 20
SEQRES 1 E 20 DT DG DT DA DC DT DC DG DT DG DT DA DC
SEQRES 2 E 20 DT DG DG DT DA DC DA
SEQRES 1 F 20 DT DG DT DA DC DC DA DG DT DA DC DA DC
SEQRES 2 F 20 DG DA DG DT DA DC DA
SEQRES 1 A 107 ALA GLN GLN SER PRO TYR SER ALA ALA MET ALA GLU GLN
SEQRES 2 A 107 ARG HIS GLN GLU TRP LEU ARG PHE VAL ASP LEU LEU LYS
SEQRES 3 A 107 ASN ALA TYR GLN ASN ASP LEU HIS LEU PRO LEU LEU ASN
SEQRES 4 A 107 LEU MET LEU THR PRO ASP GLU ARG GLU ALA LEU GLY THR
SEQRES 5 A 107 ARG VAL ARG ILE VAL GLU GLU LEU LEU ARG GLY GLU MET
SEQRES 6 A 107 SER GLN ARG GLU LEU LYS ASN GLU LEU GLY ALA GLY ILE
SEQRES 7 A 107 ALA THR ILE THR ARG GLY SER ASN SER LEU LYS ALA ALA
SEQRES 8 A 107 PRO VAL GLU LEU ARG GLN TRP LEU GLU GLU VAL LEU LEU
SEQRES 9 A 107 LYS SER ASP
SEQRES 1 B 107 ALA GLN GLN SER PRO TYR SER ALA ALA MET ALA GLU GLN
SEQRES 2 B 107 ARG HIS GLN GLU TRP LEU ARG PHE VAL ASP LEU LEU LYS
SEQRES 3 B 107 ASN ALA TYR GLN ASN ASP LEU HIS LEU PRO LEU LEU ASN
SEQRES 4 B 107 LEU MET LEU THR PRO ASP GLU ARG GLU ALA LEU GLY THR
SEQRES 5 B 107 ARG VAL ARG ILE VAL GLU GLU LEU LEU ARG GLY GLU MET
SEQRES 6 B 107 SER GLN ARG GLU LEU LYS ASN GLU LEU GLY ALA GLY ILE
SEQRES 7 B 107 ALA THR ILE THR ARG GLY SER ASN SER LEU LYS ALA ALA
SEQRES 8 B 107 PRO VAL GLU LEU ARG GLN TRP LEU GLU GLU VAL LEU LEU
SEQRES 9 B 107 LYS SER ASP
HET TRP B 109 26
HET TRP B 201 26
HETNAM TRP TRYPTOPHAN
FORMUL 5 TRP 2(C11 H12 N2 O2)
HELIX 1 1 GLN A 17 TYR A 30 1 14
HELIX 2 2 LEU A 36 LEU A 41 1 6
HELIX 3 3 ASP A 46 ARG A 63 5 18
HELIX 4 4 LEU A 71 LEU A 75 1 5
HELIX 5 5 ILE A 79 ALA A 91 1 13
HELIX 6 6 LEU A 96 VAL A 103 1 8
HELIX 7 7 LEU B 20 TYR B 30 1 11
HELIX 8 8 ARG B 48 GLY B 52 1 5
HELIX 9 9 VAL B 55 LEU B 61 1 7
HELIX 10 10 ILE B 79 ALA B 91 1 13
HELIX 11 11 VAL B 94 GLU B 102 1 9
SITE 1 AC1 12 ARG A 54 ILE A 57 THR A 81 ARG A 84
SITE 2 AC1 12 GLY A 85 MET B 42 LEU B 43 THR B 44
SITE 3 AC1 12 PRO B 45 GLU B 47 DA E 12 DC E 13
SITE 1 AC2 10 LEU A 43 THR A 44 PRO A 45 ILE B 57
SITE 2 AC2 10 THR B 81 ARG B 84 GLY B 85 LYS B 90
SITE 3 AC2 10 DA F 12 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 - b 16 2 Bytes