Header list of 1lcd.pdb file
Complete list - 23 20 Bytes
HEADER GENE REGULATION/DNA 25-MAR-93 1LCD
TITLE STRUCTURE OF THE COMPLEX OF LAC REPRESSOR HEADPIECE AND AN 11 BASE-
TITLE 2 PAIR HALF-OPERATOR DETERMINED BY NUCLEAR MAGNETIC RESONANCE
TITLE 3 SPECTROSCOPY AND RESTRAINED MOLECULAR DYNAMICS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA (5'-D(*AP*AP*TP*TP*GP*TP*GP*AP*GP*CP*G)-3');
COMPND 3 CHAIN: B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: DNA (5'-D(*CP*GP*CP*TP*CP*AP*CP*AP*AP*TP*T)-3');
COMPND 7 CHAIN: C;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 3;
COMPND 10 MOLECULE: LAC REPRESSOR;
COMPND 11 CHAIN: A;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 MOL_ID: 2;
SOURCE 4 SYNTHETIC: YES;
SOURCE 5 MOL_ID: 3;
SOURCE 6 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 7 ORGANISM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: LAC
KEYWDS GENE REGULATION/DNA, GENE REGULATION-DNA COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 3
AUTHOR V.P.CHUPRINA,J.A.C.RULLMANN,R.M.J.N.LAMERICHS,J.H.VAN BOOM,R.BOELENS,
AUTHOR 2 R.KAPTEIN
REVDAT 4 23-FEB-22 1LCD 1 REMARK LINK
REVDAT 3 24-FEB-09 1LCD 1 VERSN
REVDAT 2 01-APR-03 1LCD 1 JRNL
REVDAT 1 31-JAN-94 1LCD 0
JRNL AUTH V.P.CHUPRINA,J.A.RULLMANN,R.M.LAMERICHS,J.H.VAN BOOM,
JRNL AUTH 2 R.BOELENS,R.KAPTEIN
JRNL TITL STRUCTURE OF THE COMPLEX OF LAC REPRESSOR HEADPIECE AND AN
JRNL TITL 2 11 BASE-PAIR HALF-OPERATOR DETERMINED BY NUCLEAR MAGNETIC
JRNL TITL 3 RESONANCE SPECTROSCOPY AND RESTRAINED MOLECULAR DYNAMICS.
JRNL REF J.MOL.BIOL. V. 234 446 1993
JRNL REFN ISSN 0022-2836
JRNL PMID 8230225
JRNL DOI 10.1006/JMBI.1993.1598
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH R.M.J.N.LAMERICHS,R.BOELENS,G.A.VAN DER MAREL,J.H.VAN BOOM,
REMARK 1 AUTH 2 R.KAPTEIN
REMARK 1 TITL ASSIGNMENT OF THE 1H-NMR SPECTRUM OF A LAC REPRESSOR
REMARK 1 TITL 2 HEADPIECE-OPERATOR COMPLEX IN H2O AND IDENTIFICATION OF
REMARK 1 TITL 3 NOES. CONSEQUENCES FOR PROTEIN-DNA INTERACTION
REMARK 1 REF EUR.J.BIOCHEM. V. 194 629 1990
REMARK 1 REFN ISSN 0014-2956
REMARK 1 REFERENCE 2
REMARK 1 AUTH R.KAPTEIN,R.M.J.N.LAMERICHS,R.BOELENS,J.A.C.RULLMANN
REMARK 1 TITL TWO-DIMENSIONAL NMR STUDY OF A PROTEIN-DNA COMPLEX. LAC
REMARK 1 TITL 2 REPRESSOR HEADPIECE-OPERATOR INTERACTION
REMARK 1 REF BIOCHEM.PHARM. V. 40 89 1990
REMARK 1 REFN ISSN 0006-2952
REMARK 1 REFERENCE 3
REMARK 1 AUTH R.M.J.N.LAMERICHS,R.BOELENS,G.A.VAN DER MAREL,J.H.VAN BOOM,
REMARK 1 AUTH 2 R.KAPTEIN,F.BUCK,B.FERA,H.RUETERJANS
REMARK 1 TITL 1H NMR STUDY OF A COMPLEX BETWEEN THE LAC REPRESSOR
REMARK 1 TITL 2 HEADPIECE AND A 22 BASE PAIR SYMMETRIC LAC OPERATOR
REMARK 1 REF BIOCHEMISTRY V. 28 2985 1989
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 4
REMARK 1 AUTH J.A.C.RULLMANN,R.BOELENS,R.KAPTEIN
REMARK 1 TITL NMR BASED DOCKING STUDIES OF LAC REPRESSOR HEADPIECE ON A
REMARK 1 TITL 2 LAC OPERATOR FRAGMENT
REMARK 1 REF UCLA SYMP.MOL.CELL.BIOL., V. 95 11 1989
REMARK 1 REF 2 NEW SER.
REMARK 1 REFN ISSN 0735-9543
REMARK 1 REFERENCE 5
REMARK 1 AUTH R.BOELENS,R.M.J.N.LAMERICHS,J.A.C.RULLMANN,J.H.VAN BOOM,
REMARK 1 AUTH 2 R.KAPTEIN
REMARK 1 TITL THE INTERACTION OF LAC REPRESSOR HEADPIECE WITH ITS
REMARK 1 TITL 2 OPERATOR: AN NMR VIEW
REMARK 1 REF PROTEIN SEQ.DATA ANAL. V. 1 487 1988
REMARK 1 REFN ISSN 0931-9506
REMARK 1 REFERENCE 6
REMARK 1 AUTH J.DE VLIEG,R.M.SCHEEK,W.F.VAN GUNSTEREN,H.J.C.BERENDSEN,
REMARK 1 AUTH 2 R.KAPTEIN,J.THOMASON
REMARK 1 TITL COMBINED PROCEDURE OF DISTANCE GEOMETRY AND RESTRAINED
REMARK 1 TITL 2 MOLECULAR DYNAMICS TECHNIQUES FOR PROTEIN STRUCTURE
REMARK 1 TITL 3 DETERMINATION FROM NUCLEAR MAGNETIC RESONANCE DATA:
REMARK 1 TITL 4 APPLICATION TO THE DNA BINDING DOMAIN OF LAC REPRESSOR FROM
REMARK 1 TITL 5 ESCHERICHIA COLI
REMARK 1 REF PROTEINS V. 3 209 1988
REMARK 1 REFN ISSN 0887-3585
REMARK 1 REFERENCE 7
REMARK 1 AUTH R.BOELENS,R.M.SCHEEK,R.M.J.N.LAMERICHS,J.DE VLIEG,
REMARK 1 AUTH 2 J.H.VAN BOOM,R.KAPTEIN
REMARK 1 TITL A TWO-DIMENSIONAL NMR STUDY OF THE COMPLEX OF LAC REPRESSOR
REMARK 1 TITL 2 HEADPIECE WITH A 14 BASE PAIR LAC OPERATOR FRAGMENT
REMARK 1 REF NATO ASI SER.,SER.A V. 137 191 1987
REMARK 1 REFN ISSN 0161-0449
REMARK 1 REFERENCE 8
REMARK 1 AUTH R.BOELENS,R.M.SCHEEK,J.H.VAN BOOM,R.KAPTEIN
REMARK 1 TITL COMPLEX OF LAC REPRESSOR HEADPIECE WITH A 14 BASE PAIR LAC
REMARK 1 TITL 2 OPERATOR FRAGMENT STUDIED BY TWO-DIMENSIONAL NUCLEAR
REMARK 1 TITL 3 MAGNETIC RESONANCE
REMARK 1 REF J.MOL.BIOL. V. 193 213 1987
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 9
REMARK 1 AUTH J.DE VLIEG,R.BOELENS,R.M.SCHEEK,R.KAPTEIN,W.F.VAN GUNSTEREN
REMARK 1 TITL RESTRAINED MOLECULAR DYNAMICS PROCEDURE FOR PROTEIN TERTIARY
REMARK 1 TITL 2 STRUCTURE DETERMINATION FROM NMR DATA: A LAC REPRESSOR
REMARK 1 TITL 3 HEADPIECE STRUCTURE BASED ON INFORMATION ON J-COUPLING AND
REMARK 1 TITL 4 FROM PRESENCE AND ABSENCE OF NOES
REMARK 1 REF ISR.J.CHEM. V. 27 181 1986
REMARK 1 REFN ISSN 0021-2148
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NULL
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1LCD 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_1000174652.
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 : 3
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: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C, 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 HH TYR A 7 O HOH A 67 1.56
REMARK 500 HH TYR A 17 O HOH A 68 1.57
REMARK 500 HG SER A 31 O HOH A 63 1.59
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 DA B 1 C5 DA B 1 N7 -0.052
REMARK 500 1 DA B 1 N9 DA B 1 C4 -0.041
REMARK 500 1 DA B 2 C5 DA B 2 N7 -0.060
REMARK 500 1 DA B 2 N9 DA B 2 C4 -0.051
REMARK 500 1 DT B 3 C5 DT B 3 C6 0.055
REMARK 500 1 DT B 3 C6 DT B 3 N1 0.042
REMARK 500 1 DT B 4 C5 DT B 4 C6 0.062
REMARK 500 1 DG B 5 C5 DG B 5 N7 -0.051
REMARK 500 1 DG B 5 N7 DG B 5 C8 0.040
REMARK 500 1 DG B 5 C8 DG B 5 N9 -0.053
REMARK 500 1 DG B 5 N9 DG B 5 C4 -0.056
REMARK 500 1 DG B 7 C5 DG B 7 N7 -0.050
REMARK 500 1 DG B 7 C8 DG B 7 N9 -0.050
REMARK 500 1 DG B 7 N9 DG B 7 C4 -0.055
REMARK 500 1 DA B 8 C5 DA B 8 N7 -0.070
REMARK 500 1 DA B 8 N9 DA B 8 C4 -0.042
REMARK 500 1 DG B 9 C5 DG B 9 N7 -0.063
REMARK 500 1 DG B 9 C8 DG B 9 N9 -0.052
REMARK 500 1 DC B 10 C5 DC B 10 C6 0.064
REMARK 500 1 DG B 11 C5 DG B 11 N7 -0.052
REMARK 500 1 DG B 11 N9 DG B 11 C4 -0.051
REMARK 500 1 DC C 1 N1 DC C 1 C6 0.041
REMARK 500 1 DC C 1 C5 DC C 1 C6 0.052
REMARK 500 1 DG C 2 C5 DG C 2 N7 -0.043
REMARK 500 1 DC C 3 N1 DC C 3 C6 0.043
REMARK 500 1 DT C 4 C5 DT C 4 C6 0.064
REMARK 500 1 DC C 5 N1 DC C 5 C6 0.048
REMARK 500 1 DC C 5 C5 DC C 5 C6 0.057
REMARK 500 1 DA C 6 C5 DA C 6 N7 -0.058
REMARK 500 1 DA C 6 C8 DA C 6 N9 -0.054
REMARK 500 1 DA C 6 N9 DA C 6 C4 -0.045
REMARK 500 1 DC C 7 N1 DC C 7 C6 0.043
REMARK 500 1 DC C 7 C5 DC C 7 C6 0.061
REMARK 500 1 DA C 8 C5 DA C 8 N7 -0.048
REMARK 500 1 DA C 8 C8 DA C 8 N9 -0.051
REMARK 500 1 DA C 8 N9 DA C 8 C4 -0.040
REMARK 500 1 DA C 9 C5 DA C 9 N7 -0.059
REMARK 500 1 DA C 9 C8 DA C 9 N9 -0.050
REMARK 500 1 DA C 9 N9 DA C 9 C4 -0.046
REMARK 500 1 DT C 10 C5 DT C 10 C6 0.049
REMARK 500 1 DT C 10 C5 DT C 10 C7 0.036
REMARK 500 1 DT C 11 C5 DT C 11 C6 0.051
REMARK 500 2 DA B 1 C5 DA B 1 N7 -0.051
REMARK 500 2 DA B 1 C8 DA B 1 N9 -0.060
REMARK 500 2 DA B 1 N9 DA B 1 C4 -0.048
REMARK 500 2 DA B 2 C5 DA B 2 N7 -0.049
REMARK 500 2 DA B 2 C8 DA B 2 N9 -0.053
REMARK 500 2 DA B 2 N9 DA B 2 C4 -0.054
REMARK 500 2 DT B 3 C5 DT B 3 C6 0.058
REMARK 500 2 DT B 3 C5 DT B 3 C7 0.038
REMARK 500
REMARK 500 THIS ENTRY HAS 125 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 DA B 1 C3' - C2' - C1' ANGL. DEV. = -4.9 DEGREES
REMARK 500 1 DA B 1 N1 - C2 - N3 ANGL. DEV. = -9.7 DEGREES
REMARK 500 1 DA B 1 C2 - N3 - C4 ANGL. DEV. = 11.8 DEGREES
REMARK 500 1 DA B 1 N3 - C4 - C5 ANGL. DEV. = -7.9 DEGREES
REMARK 500 1 DA B 1 C5 - C6 - N1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 1 DA B 1 N3 - C4 - N9 ANGL. DEV. = 7.4 DEGREES
REMARK 500 1 DA B 2 N1 - C2 - N3 ANGL. DEV. = -9.7 DEGREES
REMARK 500 1 DA B 2 C2 - N3 - C4 ANGL. DEV. = 10.4 DEGREES
REMARK 500 1 DA B 2 N3 - C4 - C5 ANGL. DEV. = -5.5 DEGREES
REMARK 500 1 DA B 2 C5 - C6 - N1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 1 DA B 2 C5 - N7 - C8 ANGL. DEV. = 3.2 DEGREES
REMARK 500 1 DA B 2 N7 - C8 - N9 ANGL. DEV. = -4.1 DEGREES
REMARK 500 1 DA B 2 C8 - N9 - C4 ANGL. DEV. = 2.7 DEGREES
REMARK 500 1 DA B 2 N3 - C4 - N9 ANGL. DEV. = 4.8 DEGREES
REMARK 500 1 DA B 2 C6 - C5 - N7 ANGL. DEV. = 4.2 DEGREES
REMARK 500 1 DT B 3 C5' - C4' - O4' ANGL. DEV. = 7.7 DEGREES
REMARK 500 1 DT B 3 C1' - O4' - C4' ANGL. DEV. = -10.6 DEGREES
REMARK 500 1 DT B 3 O4' - C1' - N1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 1 DT B 3 N1 - C2 - N3 ANGL. DEV. = 4.8 DEGREES
REMARK 500 1 DT B 3 C2 - N3 - C4 ANGL. DEV. = -6.7 DEGREES
REMARK 500 1 DT B 3 N3 - C4 - C5 ANGL. DEV. = 6.0 DEGREES
REMARK 500 1 DT B 3 N3 - C2 - O2 ANGL. DEV. = -7.0 DEGREES
REMARK 500 1 DT B 3 N3 - C4 - O4 ANGL. DEV. = -4.8 DEGREES
REMARK 500 1 DT B 4 O4' - C1' - C2' ANGL. DEV. = 3.0 DEGREES
REMARK 500 1 DT B 4 N1 - C2 - N3 ANGL. DEV. = 5.7 DEGREES
REMARK 500 1 DT B 4 C2 - N3 - C4 ANGL. DEV. = -6.7 DEGREES
REMARK 500 1 DT B 4 N3 - C4 - C5 ANGL. DEV. = 5.0 DEGREES
REMARK 500 1 DT B 4 N3 - C2 - O2 ANGL. DEV. = -5.7 DEGREES
REMARK 500 1 DT B 4 N3 - C4 - O4 ANGL. DEV. = -4.8 DEGREES
REMARK 500 1 DT B 4 C5 - C4 - O4 ANGL. DEV. = -4.5 DEGREES
REMARK 500 1 DG B 5 C6 - N1 - C2 ANGL. DEV. = -6.1 DEGREES
REMARK 500 1 DG B 5 C2 - N3 - C4 ANGL. DEV. = 9.4 DEGREES
REMARK 500 1 DG B 5 N3 - C4 - C5 ANGL. DEV. = -7.2 DEGREES
REMARK 500 1 DG B 5 C5 - C6 - N1 ANGL. DEV. = 8.0 DEGREES
REMARK 500 1 DG B 5 C4 - C5 - N7 ANGL. DEV. = -4.5 DEGREES
REMARK 500 1 DG B 5 C5 - N7 - C8 ANGL. DEV. = 3.3 DEGREES
REMARK 500 1 DG B 5 N7 - C8 - N9 ANGL. DEV. = -3.2 DEGREES
REMARK 500 1 DG B 5 N9 - C4 - C5 ANGL. DEV. = 2.5 DEGREES
REMARK 500 1 DG B 5 N3 - C4 - N9 ANGL. DEV. = 4.6 DEGREES
REMARK 500 1 DG B 5 C6 - C5 - N7 ANGL. DEV. = 5.6 DEGREES
REMARK 500 1 DG B 5 C5 - C6 - O6 ANGL. DEV. = -6.3 DEGREES
REMARK 500 1 DT B 6 C2 - N3 - C4 ANGL. DEV. = -7.2 DEGREES
REMARK 500 1 DT B 6 N3 - C4 - C5 ANGL. DEV. = 6.9 DEGREES
REMARK 500 1 DT B 6 N3 - C2 - O2 ANGL. DEV. = -4.8 DEGREES
REMARK 500 1 DT B 6 C6 - C5 - C7 ANGL. DEV. = -6.7 DEGREES
REMARK 500 1 DG B 7 O4' - C1' - C2' ANGL. DEV. = -5.5 DEGREES
REMARK 500 1 DG B 7 C6 - N1 - C2 ANGL. DEV. = -6.1 DEGREES
REMARK 500 1 DG B 7 C2 - N3 - C4 ANGL. DEV. = 9.5 DEGREES
REMARK 500 1 DG B 7 N3 - C4 - C5 ANGL. DEV. = -7.2 DEGREES
REMARK 500 1 DG B 7 C5 - C6 - N1 ANGL. DEV. = 8.1 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 465 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 LYS A 2 109.85 -39.18
REMARK 500 1 SER A 28 144.36 -175.28
REMARK 500 1 MET A 42 -31.64 -39.56
REMARK 500 1 ASN A 50 -15.91 91.14
REMARK 500 2 HIS A 29 69.75 66.50
REMARK 500 2 ASN A 46 38.34 -82.06
REMARK 500 3 TYR A 17 -50.84 -22.99
REMARK 500 3 SER A 28 147.83 -173.11
REMARK 500 3 HIS A 29 72.40 59.78
REMARK 500 3 ASN A 46 -36.46 -19.68
REMARK 500 3 TYR A 47 124.90 53.23
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 DA B 1 0.08 SIDE CHAIN
REMARK 500 1 DA B 2 0.07 SIDE CHAIN
REMARK 500 1 DT B 3 0.24 SIDE CHAIN
REMARK 500 1 DT B 4 0.23 SIDE CHAIN
REMARK 500 1 DG B 5 0.15 SIDE CHAIN
REMARK 500 1 DT B 6 0.11 SIDE CHAIN
REMARK 500 1 DG B 7 0.16 SIDE CHAIN
REMARK 500 1 DA B 8 0.07 SIDE CHAIN
REMARK 500 1 DG B 11 0.12 SIDE CHAIN
REMARK 500 1 DC C 1 0.11 SIDE CHAIN
REMARK 500 1 DG C 2 0.11 SIDE CHAIN
REMARK 500 1 DC C 3 0.08 SIDE CHAIN
REMARK 500 1 DC C 5 0.14 SIDE CHAIN
REMARK 500 1 DA C 6 0.17 SIDE CHAIN
REMARK 500 1 DC C 7 0.08 SIDE CHAIN
REMARK 500 1 DA C 9 0.13 SIDE CHAIN
REMARK 500 1 DT C 10 0.15 SIDE CHAIN
REMARK 500 1 DT C 11 0.20 SIDE CHAIN
REMARK 500 1 TYR A 7 0.14 SIDE CHAIN
REMARK 500 1 TYR A 12 0.07 SIDE CHAIN
REMARK 500 1 TYR A 17 0.08 SIDE CHAIN
REMARK 500 1 TYR A 47 0.09 SIDE CHAIN
REMARK 500 2 DA B 1 0.07 SIDE CHAIN
REMARK 500 2 DA B 2 0.09 SIDE CHAIN
REMARK 500 2 DT B 3 0.09 SIDE CHAIN
REMARK 500 2 DT B 4 0.10 SIDE CHAIN
REMARK 500 2 DG B 5 0.10 SIDE CHAIN
REMARK 500 2 DT B 6 0.09 SIDE CHAIN
REMARK 500 2 DG B 7 0.12 SIDE CHAIN
REMARK 500 2 DA B 8 0.07 SIDE CHAIN
REMARK 500 2 DG B 9 0.09 SIDE CHAIN
REMARK 500 2 DC B 10 0.07 SIDE CHAIN
REMARK 500 2 DG B 11 0.12 SIDE CHAIN
REMARK 500 2 DC C 1 0.13 SIDE CHAIN
REMARK 500 2 DC C 3 0.11 SIDE CHAIN
REMARK 500 2 DT C 4 0.09 SIDE CHAIN
REMARK 500 2 DC C 5 0.07 SIDE CHAIN
REMARK 500 2 DA C 6 0.08 SIDE CHAIN
REMARK 500 2 DC C 7 0.08 SIDE CHAIN
REMARK 500 2 DA C 8 0.08 SIDE CHAIN
REMARK 500 2 DA C 9 0.07 SIDE CHAIN
REMARK 500 2 DT C 10 0.09 SIDE CHAIN
REMARK 500 2 DT C 11 0.11 SIDE CHAIN
REMARK 500 2 TYR A 7 0.09 SIDE CHAIN
REMARK 500 2 TYR A 12 0.11 SIDE CHAIN
REMARK 500 2 TYR A 47 0.14 SIDE CHAIN
REMARK 500 3 DT B 3 0.12 SIDE CHAIN
REMARK 500 3 DT B 4 0.10 SIDE CHAIN
REMARK 500 3 DG B 5 0.12 SIDE CHAIN
REMARK 500 3 DT B 6 0.17 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 66 PLANE DEVIATIONS.
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 1 TYR A 7 -10.45
REMARK 500 2 GLU A 11 -10.29
REMARK 500 2 ALA A 27 12.13
REMARK 500 2 HIS A 29 -12.13
REMARK 500 2 PRO A 49 12.22
REMARK 500 3 THR A 19 -10.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA C 12 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 DT C 4 OP1
REMARK 620 2 HOH C 923 O 87.5
REMARK 620 3 HOH A 53 O 100.4 144.8
REMARK 620 4 HOH A 57 O 102.6 128.0 84.0
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA C 12
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1LCC RELATED DB: PDB
DBREF 1LCD A 1 51 UNP P03023 LACI_ECOLI 1 51
DBREF 1LCD B 1 11 PDB 1LCD 1LCD 1 11
DBREF 1LCD C 1 11 PDB 1LCD 1LCD 1 11
SEQRES 1 B 11 DA DA DT DT DG DT DG DA DG DC DG
SEQRES 1 C 11 DC DG DC DT DC DA DC DA DA DT DT
SEQRES 1 A 51 MET LYS PRO VAL THR LEU TYR ASP VAL ALA GLU TYR ALA
SEQRES 2 A 51 GLY VAL SER TYR GLN THR VAL SER ARG VAL VAL ASN GLN
SEQRES 3 A 51 ALA SER HIS VAL SER ALA LYS THR ARG GLU LYS VAL GLU
SEQRES 4 A 51 ALA ALA MET ALA GLU LEU ASN TYR ILE PRO ASN ARG
HET NA C 12 1
HETNAM NA SODIUM ION
FORMUL 4 NA NA 1+
FORMUL 5 HOH *49(H2 O)
HELIX 1 1 THR A 5 GLY A 14 1 10
HELIX 2 2 SER A 16 ASN A 25 1 10
HELIX 3 3 SER A 31 LEU A 45 1 15
LINK OP1 DT C 4 NA NA C 12 1555 1555 2.52
LINK NA NA C 12 O HOH C 923 1555 1555 2.13
LINK NA NA C 12 O HOH A 53 1555 1555 2.10
LINK NA NA C 12 O HOH A 57 1555 1555 2.22
SITE 1 AC1 6 VAL A 24 HOH A 53 HOH A 57 DC C 3
SITE 2 AC1 6 DT C 4 HOH C 923
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 - 23 20 Bytes