Header list of 1cjg.pdb file
Complete list - v 27 2 Bytes
HEADER TRANSCRIPTION/DNA 14-APR-99 1CJG
TITLE NMR STRUCTURE OF LAC REPRESSOR HP62-DNA COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA (5'-
COMPND 3 D(*GP*AP*AP*TP*TP*GP*TP*GP*AP*GP*CP*GP*CP*TP*CP*AP*CP*AP*AP*TP*TP*C)-
COMPND 4 3');
COMPND 5 CHAIN: C, D;
COMPND 6 FRAGMENT: SYMMETRIC LAC OPERATOR;
COMPND 7 SYNONYM: SYML OPERATOR;
COMPND 8 ENGINEERED: YES;
COMPND 9 OTHER_DETAILS: THE OPERATOR IS A PALINDROME OF THE LEFT HALF OF THE
COMPND 10 WILD-TYPE OPERATOR AND LACKS THE CENTRAL BASE-PAIR;
COMPND 11 MOL_ID: 2;
COMPND 12 MOLECULE: PROTEIN (LAC REPRESSOR);
COMPND 13 CHAIN: A, B;
COMPND 14 FRAGMENT: HEADPIECE, RESIDUES 1 - 62;
COMPND 15 SYNONYM: LAC HP62;
COMPND 16 ENGINEERED: YES;
COMPND 17 OTHER_DETAILS: THE PROTEIN CONTAINS THE 62 N-TERMINAL RESIDUES (I.E.,
COMPND 18 THE DNA BINDING REGION) OF THE COMPLETE LAC REPRESSOR PROTEIN
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THE FRAGMENT IS A VARIANT OF THE WILD-TYPE OPERATOR
SOURCE 4 SEQUENCE OF THE LAC OPERON OF ESCHERICHIA COLI;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 7 ORGANISM_TAXID: 562;
SOURCE 8 GENE: LAC I, THE PART ENCODING THE 62 N-TERMINAL AMINOACIDS;
SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 10 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 11 EXPRESSION_SYSTEM_STRAIN: DH9;
SOURCE 12 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 13 EXPRESSION_SYSTEM_PLASMID: PGP1-2;PET-HP62
KEYWDS TRANSCRIPTION REGULATION, LAC OPERON, LAC REPRESSOR, HEADPIECE, LAC
KEYWDS 2 OPERATOR, TRANSCRIPTION-DNA COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 11
AUTHOR C.A.E.M.SPRONK,A.M.J.J.BONVIN,P.K.RADHA,G.MELACINI,R.BOELENS,
AUTHOR 2 R.KAPTEIN
REVDAT 4 27-NOV-19 1CJG 1 JRNL REMARK
REVDAT 3 24-FEB-09 1CJG 1 VERSN
REVDAT 2 01-APR-03 1CJG 1 JRNL
REVDAT 1 01-JAN-00 1CJG 0
JRNL AUTH C.A.SPRONK,A.M.BONVIN,P.K.RADHA,G.MELACINI,R.BOELENS,
JRNL AUTH 2 R.KAPTEIN
JRNL TITL THE SOLUTION STRUCTURE OF LAC REPRESSOR HEADPIECE 62
JRNL TITL 2 COMPLEXED TO A SYMMETRICAL LAC OPERATOR.
JRNL REF STRUCTURE FOLD.DES. V. 7 1483 1999
JRNL REFN ISSN 0969-2126
JRNL PMID 10647179
JRNL DOI 10.1016/S0969-2126(00)88339-2
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.SLIJPER,R.BOELENS,A.L.DAVIS,R.N.KONINGS,G.A.VAN DER MAREL,
REMARK 1 AUTH 2 J.H.VAN BOOM,R.KAPTEIN
REMARK 1 TITL BACKBONE AND SIDE CHAIN DYNAMICS OF LAC REPRESSOR HEADPIECE
REMARK 1 TITL 2 (1-56) AND ITS COMPLEX WITH DNA.
REMARK 1 REF BIOCHEMISTRY V. 36 249 1997
REMARK 1 REFN ISSN 0006-2960
REMARK 1 PMID 8993340
REMARK 1 DOI 10.1021/BI961670D
REMARK 1 REFERENCE 2
REMARK 1 AUTH C.A.SPRONK,M.SLIJPER,J.H.VAN BOOM,R.KAPTEIN,R.BOELENS
REMARK 1 TITL FORMATION OF THE HINGE HELIX IN THE LAC REPRESSOR IS INDUCED
REMARK 1 TITL 2 UPON BINDING TO THE LAC OPERATOR.
REMARK 1 REF NAT.STRUCT.BIOL. V. 3 916 1996
REMARK 1 REFN ISSN 1072-8368
REMARK 1 PMID 8901866
REMARK 1 DOI 10.1038/NSB1196-916
REMARK 1 REFERENCE 3
REMARK 1 AUTH M.SLIJPER,A.M.BONVIN,R.BOELENS,R.KAPTEIN
REMARK 1 TITL REFINED STRUCTURE OF LAC REPRESSOR HEADPIECE (1-56)
REMARK 1 TITL 2 DETERMINED BY RELAXATION MATRIX CALCULATIONS FROM 2D AND 3D
REMARK 1 TITL 3 NOE DATA: CHANGE OF TERTIARY STRUCTURE UPON BINDING TO THE
REMARK 1 TITL 4 LAC OPERATOR.
REMARK 1 REF J.MOL.BIOL. V. 259 761 1996
REMARK 1 REFN ISSN 0022-2836
REMARK 1 PMID 8683581
REMARK 1 DOI 10.1006/JMBI.1996.0356
REMARK 1 REFERENCE 4
REMARK 1 AUTH V.P.CHUPRINA,J.A.RULLMANN,R.M.LAMERICHS,J.H.VAN BOOM,
REMARK 1 AUTH 2 R.BOELENS,R.KAPTEIN
REMARK 1 TITL STRUCTURE OF THE COMPLEX OF LAC REPRESSOR HEADPIECE AND AN
REMARK 1 TITL 2 11 BASE-PAIR HALF-OPERATOR DETERMINED BY NUCLEAR MAGNETIC
REMARK 1 TITL 3 RESONANCE SPECTROSCOPY AND RESTRAINED MOLECULAR DYNAMICS.
REMARK 1 REF J.MOL.BIOL. V. 234 446 1993
REMARK 1 REFN ISSN 0022-2836
REMARK 1 PMID 8230225
REMARK 1 DOI 10.1006/JMBI.1993.1598
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES WERE DETERMINED BY FIRST
REMARK 3 CALCULATING THE STRUCTURE OF THE HP62 MONOMER USING THE STANDARD
REMARK 3 XPLOR PARAMETER SETS FOR NMR STRUCTURE DETERMINATION. THE HP62
REMARK 3 MONOMERS WERE SUBSEQUENTLY DUPLICATED AND DOCKED ONTO A B-DNA
REMARK 3 TEMPLATE STRUCTURE OF THE LAC OPERATOR, WHICH WAS ALLOWED TO
REMARK 3 BEND IN ORDER TO ACCOMODATE THE TWO HP62 MONOMERS. THE PROPERLY
REMARK 3 DOCKED STRUCTURES WERE PLACED IN A TIP3P WATERBOX WHICH WAS
REMARK 3 NEUTRALIZED BY ADDITION OF SODIUM-IONS. THE STRUCTURES WERE THEN
REMARK 3 FURTHER REFINED BY A RESTRAINED MD SIMULATION OF 24 PS IN THE
REMARK 3 CHARMM22 FORCEFIELD FOR PROTEINS AND NUCLEIC ACIDS. NCS SYMMETRY
REMARK 3 RESTRAINTS WERE USED DURING THE DOCKING AND REFINEMENT
REMARK 3 PROCEDURES. FOR FURTHER REFINEMENT DETAILS SEE THE PAPER
REMARK 3 DESCRIBING THE STRUCTURES
REMARK 4
REMARK 4 1CJG COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-APR-99.
REMARK 100 THE DEPOSITION ID IS D_1000000848.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 315
REMARK 210 PH : 6.1
REMARK 210 IONIC STRENGTH : SEE ARTICLE
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : SEE ARTICLE
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : SEE ARTICLE
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR 3.851
REMARK 210 METHOD USED : SIMULATED ANNEALING FOLLOWED BY
REMARK 210 RESTRAINED MD
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 14
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 11
REMARK 210 CONFORMERS, SELECTION CRITERIA : SEE ARTICLE
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: RESONANCE ASSIGNMENTS WERE BASED ON VARIOUS HOMONUCLEAR
REMARK 210 AND DOUBLE AND TRIPLE RESONANCE NMR EXPERIMENTS IN H2O/D2O (95%/
REMARK 210 5%) AND D2O. IN ADDITION ISOTOPE FILTER EXPERIMENTS WERE APPLIED
REMARK 210 TO OBTAIN ADDITIONAL ASSIGNMENTS AND TO ASSIGN INTER-MOLECULAR
REMARK 210 NOES. FOR FURTHER DETAILS SEE THE REFERENCE DESCRIBING THE
REMARK 210 STRUCTURES
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: C, D, 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 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 7 DG C 1 C5 DG C 1 C6 -0.060
REMARK 500 8 DG C 12 C5 DG C 12 C6 -0.060
REMARK 500 10 DG D 6 C5 DG D 6 C6 -0.060
REMARK 500 11 DG D 1 C5 DG D 1 C6 -0.060
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 DG C 1 N3 - C2 - N2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 1 DG C 6 N3 - C2 - N2 ANGL. DEV. = 4.6 DEGREES
REMARK 500 1 DG C 8 N3 - C2 - N2 ANGL. DEV. = 6.6 DEGREES
REMARK 500 1 DA C 9 O4' - C1' - C2' ANGL. DEV. = -5.0 DEGREES
REMARK 500 1 DA C 9 O4' - C1' - N9 ANGL. DEV. = 2.7 DEGREES
REMARK 500 1 DG C 10 N3 - C2 - N2 ANGL. DEV. = 5.0 DEGREES
REMARK 500 1 DG C 12 O4' - C1' - N9 ANGL. DEV. = 2.7 DEGREES
REMARK 500 1 DG C 12 N1 - C2 - N2 ANGL. DEV. = -5.7 DEGREES
REMARK 500 1 DG C 12 N3 - C2 - N2 ANGL. DEV. = 8.5 DEGREES
REMARK 500 1 DC C 13 O4' - C1' - N1 ANGL. DEV. = 5.0 DEGREES
REMARK 500 1 DC C 13 N3 - C2 - O2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 1 DT C 20 O4' - C1' - N1 ANGL. DEV. = 2.8 DEGREES
REMARK 500 1 DG D 1 N3 - C2 - N2 ANGL. DEV. = 4.9 DEGREES
REMARK 500 1 DG D 6 N3 - C2 - N2 ANGL. DEV. = 4.6 DEGREES
REMARK 500 1 DG D 8 N1 - C2 - N3 ANGL. DEV. = -4.2 DEGREES
REMARK 500 1 DG D 8 N3 - C2 - N2 ANGL. DEV. = 7.7 DEGREES
REMARK 500 1 DA D 9 O4' - C1' - C2' ANGL. DEV. = -4.8 DEGREES
REMARK 500 1 DA D 9 O4' - C1' - N9 ANGL. DEV. = 3.6 DEGREES
REMARK 500 1 DG D 10 N3 - C2 - N2 ANGL. DEV. = 4.3 DEGREES
REMARK 500 1 DG D 12 O4' - C1' - N9 ANGL. DEV. = 1.9 DEGREES
REMARK 500 1 DG D 12 N3 - C2 - N2 ANGL. DEV. = 5.1 DEGREES
REMARK 500 1 DC D 13 O4' - C1' - N1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 1 DC D 13 N3 - C2 - O2 ANGL. DEV. = -4.6 DEGREES
REMARK 500 1 DT D 20 O4' - C1' - N1 ANGL. DEV. = 2.3 DEGREES
REMARK 500 1 ARG A 22 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 1 TYR A 47 CB - CG - CD2 ANGL. DEV. = -5.2 DEGREES
REMARK 500 1 TYR A 47 CB - CG - CD1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 1 ARG A 51 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 1 MET B 42 CG - SD - CE ANGL. DEV. = -11.9 DEGREES
REMARK 500 1 TYR B 47 CB - CG - CD2 ANGL. DEV. = -5.3 DEGREES
REMARK 500 1 TYR B 47 CB - CG - CD1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 2 DG C 1 N3 - C2 - N2 ANGL. DEV. = 5.1 DEGREES
REMARK 500 2 DT C 4 O4' - C1' - N1 ANGL. DEV. = 1.8 DEGREES
REMARK 500 2 DG C 6 N3 - C2 - N2 ANGL. DEV. = 5.6 DEGREES
REMARK 500 2 DG C 8 N3 - C2 - N2 ANGL. DEV. = 7.5 DEGREES
REMARK 500 2 DG C 10 O4' - C1' - N9 ANGL. DEV. = 2.0 DEGREES
REMARK 500 2 DG C 10 N3 - C2 - N2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 2 DG C 12 N1 - C2 - N3 ANGL. DEV. = -3.6 DEGREES
REMARK 500 2 DG C 12 C8 - N9 - C4 ANGL. DEV. = -2.4 DEGREES
REMARK 500 2 DG C 12 N1 - C2 - N2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 2 DG C 12 N3 - C2 - N2 ANGL. DEV. = 9.6 DEGREES
REMARK 500 2 DC C 13 O4' - C1' - N1 ANGL. DEV. = 2.9 DEGREES
REMARK 500 2 DG D 1 N3 - C2 - N2 ANGL. DEV. = 6.9 DEGREES
REMARK 500 2 DG D 6 N3 - C2 - N2 ANGL. DEV. = 6.4 DEGREES
REMARK 500 2 DG D 8 N1 - C2 - N3 ANGL. DEV. = -3.6 DEGREES
REMARK 500 2 DG D 8 N3 - C2 - N2 ANGL. DEV. = 7.8 DEGREES
REMARK 500 2 DG D 10 N3 - C2 - N2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 2 DG D 12 N3 - C2 - N2 ANGL. DEV. = 7.5 DEGREES
REMARK 500 2 DC D 13 O4' - C1' - N1 ANGL. DEV. = 2.9 DEGREES
REMARK 500 2 DT D 20 O4' - C1' - N1 ANGL. DEV. = 2.0 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 299 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 VAL A 15 -170.00 -124.98
REMARK 500 1 SER A 28 -64.93 -108.34
REMARK 500 1 VAL A 30 -100.22 -126.29
REMARK 500 1 SER A 31 170.49 178.59
REMARK 500 1 ASN A 46 71.16 73.96
REMARK 500 1 LYS A 59 138.90 53.94
REMARK 500 1 SER B 28 -73.37 -102.17
REMARK 500 1 VAL B 30 -96.67 -128.21
REMARK 500 1 SER B 31 167.80 175.27
REMARK 500 1 ASN B 46 71.21 72.56
REMARK 500 1 LYS B 59 143.32 58.63
REMARK 500 2 PRO A 3 146.35 -37.18
REMARK 500 2 GLN A 26 74.70 56.09
REMARK 500 2 SER A 28 -77.38 -72.09
REMARK 500 2 TYR A 47 114.52 -37.16
REMARK 500 2 SER A 61 -72.21 -90.86
REMARK 500 2 VAL B 15 -164.40 -127.43
REMARK 500 2 GLN B 26 76.69 67.24
REMARK 500 2 SER B 28 -72.93 -82.68
REMARK 500 2 SER B 61 -74.85 -95.79
REMARK 500 3 ASN A 46 66.73 73.71
REMARK 500 3 ALA A 57 -79.78 -67.05
REMARK 500 3 LYS A 59 124.60 70.02
REMARK 500 3 ALA B 27 87.05 -68.74
REMARK 500 3 ASN B 46 66.27 69.44
REMARK 500 3 ALA B 57 -73.78 -67.99
REMARK 500 3 LYS B 59 127.39 95.08
REMARK 500 4 SER A 28 -72.31 -163.59
REMARK 500 4 ALA A 32 -50.95 70.24
REMARK 500 4 ASN A 46 63.12 66.65
REMARK 500 4 ASN B 25 -66.01 -108.51
REMARK 500 4 SER B 28 -77.07 -160.70
REMARK 500 4 ALA B 32 -49.75 71.55
REMARK 500 4 ASN B 46 69.64 69.35
REMARK 500 5 ASN A 25 -21.01 -150.21
REMARK 500 5 ALA A 27 93.93 -60.71
REMARK 500 5 SER A 28 -96.86 -142.62
REMARK 500 5 ASN A 46 62.39 65.06
REMARK 500 5 ARG A 51 40.12 -80.51
REMARK 500 5 SER A 61 -108.62 58.67
REMARK 500 5 ASN B 25 -7.27 -149.56
REMARK 500 5 GLN B 26 54.72 -93.56
REMARK 500 5 ALA B 27 87.44 -60.16
REMARK 500 5 SER B 28 -98.50 -136.27
REMARK 500 5 ARG B 51 45.12 -81.31
REMARK 500 5 ALA B 57 -19.73 -49.34
REMARK 500 5 SER B 61 -106.75 44.09
REMARK 500 6 LYS A 2 -63.98 -152.19
REMARK 500 6 ASN A 46 67.31 69.84
REMARK 500 6 PRO A 49 107.88 -53.26
REMARK 500
REMARK 500 THIS ENTRY HAS 96 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 ILE A 48 PRO A 49 3 149.46
REMARK 500 LYS A 2 PRO A 3 9 141.33
REMARK 500 LYS B 2 PRO B 3 9 144.50
REMARK 500 LYS A 2 PRO A 3 10 144.67
REMARK 500 LYS B 2 PRO B 3 10 143.94
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 C 4 0.08 SIDE CHAIN
REMARK 500 1 DC C 11 0.09 SIDE CHAIN
REMARK 500 1 DG C 12 0.08 SIDE CHAIN
REMARK 500 1 DC C 13 0.07 SIDE CHAIN
REMARK 500 1 DT C 14 0.09 SIDE CHAIN
REMARK 500 1 DC C 22 0.10 SIDE CHAIN
REMARK 500 1 DG D 8 0.06 SIDE CHAIN
REMARK 500 1 DC D 11 0.09 SIDE CHAIN
REMARK 500 1 DG D 12 0.07 SIDE CHAIN
REMARK 500 1 DT D 14 0.08 SIDE CHAIN
REMARK 500 1 DC D 22 0.11 SIDE CHAIN
REMARK 500 1 ARG A 35 0.11 SIDE CHAIN
REMARK 500 1 ARG B 22 0.08 SIDE CHAIN
REMARK 500 1 ARG B 35 0.10 SIDE CHAIN
REMARK 500 2 DT C 7 0.07 SIDE CHAIN
REMARK 500 2 DG C 8 0.06 SIDE CHAIN
REMARK 500 2 DA C 9 0.05 SIDE CHAIN
REMARK 500 2 DC C 13 0.06 SIDE CHAIN
REMARK 500 2 DT C 14 0.07 SIDE CHAIN
REMARK 500 2 DG D 1 0.07 SIDE CHAIN
REMARK 500 2 DG D 8 0.08 SIDE CHAIN
REMARK 500 2 DT D 14 0.06 SIDE CHAIN
REMARK 500 2 DA D 19 0.06 SIDE CHAIN
REMARK 500 2 DC D 22 0.10 SIDE CHAIN
REMARK 500 3 DA C 9 0.06 SIDE CHAIN
REMARK 500 3 DT C 14 0.07 SIDE CHAIN
REMARK 500 3 DC C 17 0.06 SIDE CHAIN
REMARK 500 3 DT D 4 0.07 SIDE CHAIN
REMARK 500 3 DA D 9 0.06 SIDE CHAIN
REMARK 500 3 DC D 15 0.06 SIDE CHAIN
REMARK 500 3 DC D 17 0.07 SIDE CHAIN
REMARK 500 3 DC D 22 0.08 SIDE CHAIN
REMARK 500 3 HIS A 29 0.08 SIDE CHAIN
REMARK 500 3 TYR B 12 0.08 SIDE CHAIN
REMARK 500 4 DG C 1 0.07 SIDE CHAIN
REMARK 500 4 DA C 2 0.05 SIDE CHAIN
REMARK 500 4 DT C 7 0.06 SIDE CHAIN
REMARK 500 4 DG C 8 0.07 SIDE CHAIN
REMARK 500 4 DG C 12 0.08 SIDE CHAIN
REMARK 500 4 DA C 16 0.06 SIDE CHAIN
REMARK 500 4 DC C 22 0.08 SIDE CHAIN
REMARK 500 4 DG D 1 0.08 SIDE CHAIN
REMARK 500 4 DT D 7 0.07 SIDE CHAIN
REMARK 500 4 DG D 8 0.07 SIDE CHAIN
REMARK 500 4 DC D 11 0.06 SIDE CHAIN
REMARK 500 4 DA D 16 0.07 SIDE CHAIN
REMARK 500 4 DC D 22 0.10 SIDE CHAIN
REMARK 500 4 HIS A 29 0.08 SIDE CHAIN
REMARK 500 4 HIS B 29 0.08 SIDE CHAIN
REMARK 500 5 DG C 1 0.08 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 119 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1CJG A 1 62 UNP P03023 LACI_ECOLI 1 62
DBREF 1CJG B 1 62 UNP P03023 LACI_ECOLI 1 62
DBREF 1CJG C 1 22 PDB 1CJG 1CJG 1 22
DBREF 1CJG D 1 22 PDB 1CJG 1CJG 1 22
SEQRES 1 C 22 DG DA DA DT DT DG DT DG DA DG DC DG DC
SEQRES 2 C 22 DT DC DA DC DA DA DT DT DC
SEQRES 1 D 22 DG DA DA DT DT DG DT DG DA DG DC DG DC
SEQRES 2 D 22 DT DC DA DC DA DA DT DT DC
SEQRES 1 A 62 MET LYS PRO VAL THR LEU TYR ASP VAL ALA GLU TYR ALA
SEQRES 2 A 62 GLY VAL SER TYR GLN THR VAL SER ARG VAL VAL ASN GLN
SEQRES 3 A 62 ALA SER HIS VAL SER ALA LYS THR ARG GLU LYS VAL GLU
SEQRES 4 A 62 ALA ALA MET ALA GLU LEU ASN TYR ILE PRO ASN ARG VAL
SEQRES 5 A 62 ALA GLN GLN LEU ALA GLY LYS GLN SER LEU
SEQRES 1 B 62 MET LYS PRO VAL THR LEU TYR ASP VAL ALA GLU TYR ALA
SEQRES 2 B 62 GLY VAL SER TYR GLN THR VAL SER ARG VAL VAL ASN GLN
SEQRES 3 B 62 ALA SER HIS VAL SER ALA LYS THR ARG GLU LYS VAL GLU
SEQRES 4 B 62 ALA ALA MET ALA GLU LEU ASN TYR ILE PRO ASN ARG VAL
SEQRES 5 B 62 ALA GLN GLN LEU ALA GLY LYS GLN SER LEU
HELIX 1 1 LEU A 6 ALA A 13 1 8
HELIX 2 2 TYR A 17 VAL A 24 1 8
HELIX 3 3 ALA A 32 LEU A 45 1 14
HELIX 4 4 ARG A 51 LEU A 56 1 6
HELIX 5 5 LEU B 6 ALA B 13 1 8
HELIX 6 6 TYR B 17 VAL B 24 1 8
HELIX 7 7 ALA B 32 GLU B 44 1 13
HELIX 8 8 ARG B 51 LEU B 56 1 6
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 - v 27 2 Bytes