Header list of 1lqc.pdb file
Complete list - b 23 2 Bytes
HEADER TRANSCRIPTION REGULATION 13-AUG-96 1LQC TITLE LAC REPRESSOR HEADPIECE (RESIDUES 1-56), NMR, 32 STRUCTURES COMPND MOL_ID: 1; COMPND 2 MOLECULE: LAC REPRESSOR; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: HEADPIECE, RESIDUES 1 - 56; COMPND 5 SYNONYM: LAC HP56; COMPND 6 ENGINEERED: YES; COMPND 7 OTHER_DETAILS: THE PROTEIN CONTAINS THE FIRST 56 N-TERMINAL RESIDUES COMPND 8 (I.E., THE DNA BINDING REGION) OF THE COMPLETE LAC REPRESSOR PROTEIN SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI; SOURCE 3 ORGANISM_TAXID: 562; SOURCE 4 VARIANT: DH9; SOURCE 5 GENE: LAC I THE PART ENCODING ONLY; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: LAC; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET-HP56; SOURCE 10 EXPRESSION_SYSTEM_GENE: LAC I, THE PART ENCODING ONLY THE FIRST 56 SOURCE 11 AMINO ACIDS; SOURCE 12 OTHER_DETAILS: T7 RNA POLYMERASE PROMOTER SYSTEM KEYWDS TRANSCRIPTION REGULATION, LAC OPERON, LAC REPRESSOR, HEADPIECE, DNA EXPDTA SOLUTION NMR NUMMDL 32 AUTHOR M.SLIJPER,A.M.J.J.BONVIN,R.BOELENS,R.KAPTEIN REVDAT 3 23-FEB-22 1LQC 1 REMARK REVDAT 2 24-FEB-09 1LQC 1 VERSN REVDAT 1 12-FEB-97 1LQC 0 JRNL AUTH M.SLIJPER,A.M.BONVIN,R.BOELENS,R.KAPTEIN JRNL TITL REFINED STRUCTURE OF LAC REPRESSOR HEADPIECE (1-56) JRNL TITL 2 DETERMINED BY RELAXATION MATRIX CALCULATIONS FROM 2D AND 3D JRNL TITL 3 NOE DATA: CHANGE OF TERTIARY STRUCTURE UPON BINDING TO THE JRNL TITL 4 LAC OPERATOR. JRNL REF J.MOL.BIOL. V. 259 761 1996 JRNL REFN ISSN 0022-2836 JRNL PMID 8683581 JRNL DOI 10.1006/JMBI.1996.0356 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH M.SLIJPER,R.BOELENS,A.L.DAVIS,R.N.H.KONINGS, REMARK 1 AUTH 2 G.A.VAN DER MAREL,J.H.VAN BLOOM REMARK 1 TITL BACKBONE AND SIDECHAIN DYNAMICS OF LAC REPRESSOR HEADPIECE REMARK 1 TITL 2 (1-56) AND ITS COMPLEX WITH DNA REMARK 1 REF TO BE PUBLISHED REMARK 1 REFN REMARK 1 REFERENCE 2 REMARK 1 AUTH M.SLIJPER,M.J.J.BONVIN,R.BOELENS,R.KAPTEIN REMARK 1 TITL APPLICATION OF STRUCTURE REFINEMENT USING 3D NOE-NOE REMARK 1 TITL 2 SPECTROSCOPY TO LAC REPRESSOR HEADPIECE (1-56) REMARK 1 REF J.MAGN.RESON.,SER.B V. 107 298 1995 REMARK 1 REFN ISSN 1064-1866 REMARK 1 REFERENCE 3 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 REFERENCE 4 REMARK 1 AUTH E.R.ZUIDERWEG,R.M.SCHEEK,R.KAPTEIN REMARK 1 TITL TWO-DIMENSIONAL 1H-NMR STUDIES ON THE LAC REPRESSOR DNA REMARK 1 TITL 2 BINDING DOMAIN: FURTHER RESONANCE ASSIGNMENTS AND REMARK 1 TITL 3 IDENTIFICATION OF NUCLEAR OVERHAUSER ENHANCEMENTS REMARK 1 REF BIOPOLYMERS V. 24 2257 1985 REMARK 1 REFN ISSN 0006-3525 REMARK 1 REFERENCE 5 REMARK 1 AUTH E.R.P.ZUIDERWEG,R.BOELENS,R.KAPTEIN REMARK 1 TITL STEREOSPECIFIC ASSIGNMENTS OF 1H-NMR METHYL LINES AND REMARK 1 TITL 2 CONFORMATION OF VALYL RESIDUES IN THE LAC REPRESSOR REMARK 1 TITL 3 HEADPIECE REMARK 1 REF BIOPOLYMERS V. 24 601 1985 REMARK 1 REFN ISSN 0006-3525 REMARK 1 REFERENCE 6 REMARK 1 AUTH E.R.ZUIDERWEG,R.KAPTEIN,K.WUTHRICH REMARK 1 TITL SEQUENCE-SPECIFIC RESONANCE ASSIGNMENTS IN THE 1H REMARK 1 TITL 2 NUCLEAR-MAGNETIC-RESONANCE SPECTRUM OF THE LAC REPRESSOR REMARK 1 TITL 3 DNA-BINDING DOMAIN 1-51 FROM ESCHERICHIA COLI BY REMARK 1 TITL 4 TWO-DIMENSIONAL SPECTROSCOPY REMARK 1 REF EUR.J.BIOCHEM. V. 137 279 1983 REMARK 1 REFN ISSN 0014-2956 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : DINOSAUR REMARK 3 AUTHORS : BONVIN,VIS,BREG,BURGERING,BOELENS,KAPTEIN REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1LQC 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_1000174799. 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 : 32 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 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (RES=RESIDUE NAME; REMARK 470 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 470 MODELS 1-32 REMARK 470 RES CSSEQI ATOMS REMARK 470 LEU A 56 O 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 22 HIS A 29 NE2 HIS A 29 CD2 -0.066 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 VAL A 4 N - CA - CB ANGL. DEV. = -14.0 DEGREES REMARK 500 1 VAL A 4 CG1 - CB - CG2 ANGL. DEV. = -10.0 DEGREES REMARK 500 1 TYR A 12 CB - CG - CD1 ANGL. DEV. = -5.4 DEGREES REMARK 500 1 TYR A 17 CB - CG - CD1 ANGL. DEV. = -6.4 DEGREES REMARK 500 1 THR A 19 CA - CB - OG1 ANGL. DEV. = 13.8 DEGREES REMARK 500 1 ARG A 22 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES REMARK 500 1 VAL A 38 CG1 - CB - CG2 ANGL. DEV. = -9.7 DEGREES REMARK 500 1 TYR A 47 CB - CG - CD2 ANGL. DEV. = -7.6 DEGREES REMARK 500 1 TYR A 47 CB - CG - CD1 ANGL. DEV. = 4.2 DEGREES REMARK 500 1 ARG A 51 NE - CZ - NH1 ANGL. DEV. = 5.7 DEGREES REMARK 500 2 VAL A 4 N - CA - CB ANGL. DEV. = -15.2 DEGREES REMARK 500 2 THR A 5 CA - CB - CG2 ANGL. DEV. = -9.2 DEGREES REMARK 500 2 TYR A 7 CB - CG - CD1 ANGL. DEV. = -4.2 DEGREES REMARK 500 2 TYR A 12 CB - CG - CD1 ANGL. DEV. = -4.7 DEGREES REMARK 500 2 TYR A 17 CB - CG - CD2 ANGL. DEV. = -6.3 DEGREES REMARK 500 2 THR A 19 CA - CB - OG1 ANGL. DEV. = 17.3 DEGREES REMARK 500 2 THR A 19 CA - CB - CG2 ANGL. DEV. = 10.9 DEGREES REMARK 500 2 ARG A 22 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES REMARK 500 2 VAL A 30 CA - CB - CG1 ANGL. DEV. = 10.5 DEGREES REMARK 500 2 VAL A 38 CG1 - CB - CG2 ANGL. DEV. = -10.3 DEGREES REMARK 500 2 TYR A 47 CB - CG - CD1 ANGL. DEV. = -4.6 DEGREES REMARK 500 2 ARG A 51 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES REMARK 500 3 VAL A 4 N - CA - CB ANGL. DEV. = -14.4 DEGREES REMARK 500 3 VAL A 4 CG1 - CB - CG2 ANGL. DEV. = -10.3 DEGREES REMARK 500 3 TYR A 7 N - CA - CB ANGL. DEV. = 11.8 DEGREES REMARK 500 3 TYR A 12 CB - CG - CD1 ANGL. DEV. = -5.1 DEGREES REMARK 500 3 TYR A 17 CB - CG - CD2 ANGL. DEV. = -4.8 DEGREES REMARK 500 3 VAL A 38 CG1 - CB - CG2 ANGL. DEV. = -10.2 DEGREES REMARK 500 3 TYR A 47 CB - CG - CD2 ANGL. DEV. = 4.5 DEGREES REMARK 500 3 TYR A 47 CB - CG - CD1 ANGL. DEV. = -9.7 DEGREES REMARK 500 4 VAL A 4 N - CA - CB ANGL. DEV. = -17.5 DEGREES REMARK 500 4 VAL A 4 CG1 - CB - CG2 ANGL. DEV. = -10.3 DEGREES REMARK 500 4 LEU A 6 CB - CG - CD1 ANGL. DEV. = 11.0 DEGREES REMARK 500 4 TYR A 7 CB - CG - CD1 ANGL. DEV. = -4.4 DEGREES REMARK 500 4 TYR A 12 CB - CG - CD1 ANGL. DEV. = -5.7 DEGREES REMARK 500 4 TYR A 17 CB - CG - CD1 ANGL. DEV. = -4.5 DEGREES REMARK 500 4 ARG A 22 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES REMARK 500 4 VAL A 38 CG1 - CB - CG2 ANGL. DEV. = -10.3 DEGREES REMARK 500 4 TYR A 47 CB - CG - CD2 ANGL. DEV. = -6.9 DEGREES REMARK 500 5 VAL A 4 N - CA - CB ANGL. DEV. = -15.3 DEGREES REMARK 500 5 VAL A 4 CA - CB - CG2 ANGL. DEV. = 9.2 DEGREES REMARK 500 5 TYR A 7 CB - CG - CD1 ANGL. DEV. = -3.9 DEGREES REMARK 500 5 TYR A 12 CB - CG - CD1 ANGL. DEV. = -4.4 DEGREES REMARK 500 5 VAL A 38 CG1 - CB - CG2 ANGL. DEV. = -11.8 DEGREES REMARK 500 5 TYR A 47 CB - CG - CD2 ANGL. DEV. = -8.9 DEGREES REMARK 500 5 TYR A 47 CB - CG - CD1 ANGL. DEV. = 4.8 DEGREES REMARK 500 5 GLN A 55 CB - CA - C ANGL. DEV. = 12.8 DEGREES REMARK 500 5 GLN A 55 CA - C - N ANGL. DEV. = -15.4 DEGREES REMARK 500 6 THR A 5 N - CA - CB ANGL. DEV. = -12.5 DEGREES REMARK 500 6 TYR A 7 CB - CG - CD1 ANGL. DEV. = -3.7 DEGREES REMARK 500 REMARK 500 THIS ENTRY HAS 296 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 2 162.71 159.49 REMARK 500 1 THR A 5 97.02 -60.00 REMARK 500 1 LEU A 6 -19.96 -39.95 REMARK 500 1 ALA A 27 40.96 29.06 REMARK 500 1 SER A 28 -52.96 56.59 REMARK 500 1 PRO A 49 -62.78 -14.54 REMARK 500 1 GLN A 55 -50.42 -169.75 REMARK 500 2 LEU A 6 -19.91 -48.69 REMARK 500 2 SER A 16 128.65 -36.65 REMARK 500 2 GLN A 26 -0.36 58.47 REMARK 500 2 SER A 28 -54.04 59.96 REMARK 500 2 PRO A 49 87.64 -44.77 REMARK 500 2 ASN A 50 -61.88 -163.97 REMARK 500 2 ARG A 51 104.41 54.57 REMARK 500 2 GLN A 55 -50.08 -163.02 REMARK 500 3 SER A 16 127.11 -7.62 REMARK 500 3 ALA A 27 38.63 26.66 REMARK 500 3 SER A 28 -50.16 58.88 REMARK 500 3 PRO A 49 85.78 -50.61 REMARK 500 3 ASN A 50 -110.40 -179.92 REMARK 500 3 ARG A 51 -10.26 39.24 REMARK 500 4 SER A 16 143.55 -27.47 REMARK 500 4 GLN A 26 -5.46 73.92 REMARK 500 4 ALA A 27 36.32 36.69 REMARK 500 4 SER A 28 -48.37 55.31 REMARK 500 4 ILE A 48 117.82 -28.10 REMARK 500 4 PRO A 49 64.99 -65.86 REMARK 500 4 ALA A 53 82.83 53.67 REMARK 500 5 SER A 16 129.63 -32.20 REMARK 500 5 ALA A 27 35.25 39.59 REMARK 500 5 SER A 28 -44.95 62.52 REMARK 500 5 HIS A 29 116.75 -165.51 REMARK 500 5 LYS A 33 -37.47 -39.69 REMARK 500 5 ASN A 46 19.05 53.92 REMARK 500 5 ILE A 48 118.85 -22.20 REMARK 500 5 PRO A 49 36.48 -52.96 REMARK 500 5 ASN A 50 123.75 -178.53 REMARK 500 5 ARG A 51 35.85 -76.25 REMARK 500 5 VAL A 52 53.81 -116.58 REMARK 500 5 GLN A 54 -91.40 44.42 REMARK 500 5 GLN A 55 69.72 -108.47 REMARK 500 6 THR A 5 109.17 -51.85 REMARK 500 6 SER A 16 121.42 -29.41 REMARK 500 6 ALA A 27 33.68 34.25 REMARK 500 6 SER A 28 -42.75 58.84 REMARK 500 6 ILE A 48 110.89 -10.08 REMARK 500 6 PRO A 49 50.71 -63.48 REMARK 500 6 ASN A 50 148.02 -179.75 REMARK 500 6 ARG A 51 95.66 -68.77 REMARK 500 6 GLN A 54 76.80 51.99 REMARK 500 REMARK 500 THIS ENTRY HAS 292 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 ARG A 51 VAL A 52 3 145.51 REMARK 500 VAL A 52 ALA A 53 3 140.38 REMARK 500 LYS A 2 PRO A 3 8 -148.78 REMARK 500 ASN A 50 ARG A 51 8 144.51 REMARK 500 GLN A 54 GLN A 55 8 149.25 REMARK 500 LYS A 2 PRO A 3 13 141.44 REMARK 500 ASN A 50 ARG A 51 14 146.23 REMARK 500 LYS A 2 PRO A 3 18 -135.17 REMARK 500 LYS A 2 PRO A 3 20 -130.27 REMARK 500 ARG A 51 VAL A 52 20 -148.39 REMARK 500 ASN A 50 ARG A 51 23 126.88 REMARK 500 ARG A 51 VAL A 52 23 145.62 REMARK 500 HIS A 29 VAL A 30 24 129.10 REMARK 500 ALA A 27 SER A 28 25 -148.45 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 12 0.09 SIDE CHAIN REMARK 500 1 TYR A 17 0.10 SIDE CHAIN REMARK 500 1 ARG A 22 0.08 SIDE CHAIN REMARK 500 2 TYR A 7 0.11 SIDE CHAIN REMARK 500 2 TYR A 12 0.12 SIDE CHAIN REMARK 500 2 TYR A 17 0.26 SIDE CHAIN REMARK 500 2 ARG A 51 0.17 SIDE CHAIN REMARK 500 3 TYR A 7 0.13 SIDE CHAIN REMARK 500 3 TYR A 12 0.10 SIDE CHAIN REMARK 500 3 TYR A 17 0.08 SIDE CHAIN REMARK 500 3 TYR A 47 0.07 SIDE CHAIN REMARK 500 4 TYR A 7 0.07 SIDE CHAIN REMARK 500 4 TYR A 12 0.08 SIDE CHAIN REMARK 500 4 TYR A 17 0.09 SIDE CHAIN REMARK 500 4 TYR A 47 0.16 SIDE CHAIN REMARK 500 6 TYR A 7 0.10 SIDE CHAIN REMARK 500 6 TYR A 12 0.09 SIDE CHAIN REMARK 500 6 TYR A 17 0.14 SIDE CHAIN REMARK 500 6 TYR A 47 0.10 SIDE CHAIN REMARK 500 7 TYR A 12 0.12 SIDE CHAIN REMARK 500 7 TYR A 17 0.12 SIDE CHAIN REMARK 500 8 TYR A 7 0.09 SIDE CHAIN REMARK 500 8 TYR A 12 0.16 SIDE CHAIN REMARK 500 8 TYR A 17 0.06 SIDE CHAIN REMARK 500 9 TYR A 7 0.11 SIDE CHAIN REMARK 500 9 TYR A 12 0.08 SIDE CHAIN REMARK 500 9 TYR A 17 0.28 SIDE CHAIN REMARK 500 10 TYR A 12 0.11 SIDE CHAIN REMARK 500 10 TYR A 17 0.08 SIDE CHAIN REMARK 500 10 TYR A 47 0.10 SIDE CHAIN REMARK 500 11 TYR A 7 0.07 SIDE CHAIN REMARK 500 11 TYR A 12 0.07 SIDE CHAIN REMARK 500 11 ARG A 51 0.12 SIDE CHAIN REMARK 500 12 TYR A 7 0.09 SIDE CHAIN REMARK 500 12 TYR A 17 0.10 SIDE CHAIN REMARK 500 13 TYR A 12 0.12 SIDE CHAIN REMARK 500 13 TYR A 17 0.13 SIDE CHAIN REMARK 500 13 TYR A 47 0.15 SIDE CHAIN REMARK 500 14 TYR A 7 0.11 SIDE CHAIN REMARK 500 14 ARG A 51 0.08 SIDE CHAIN REMARK 500 15 TYR A 7 0.09 SIDE CHAIN REMARK 500 15 TYR A 12 0.09 SIDE CHAIN REMARK 500 15 TYR A 17 0.10 SIDE CHAIN REMARK 500 15 TYR A 47 0.17 SIDE CHAIN REMARK 500 16 TYR A 7 0.09 SIDE CHAIN REMARK 500 16 TYR A 12 0.12 SIDE CHAIN REMARK 500 16 TYR A 17 0.11 SIDE CHAIN REMARK 500 16 TYR A 47 0.07 SIDE CHAIN REMARK 500 17 TYR A 12 0.10 SIDE CHAIN REMARK 500 17 ARG A 35 0.10 SIDE CHAIN REMARK 500 REMARK 500 THIS ENTRY HAS 94 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 VAL A 9 -10.18 REMARK 500 1 LYS A 33 -10.26 REMARK 500 1 ARG A 35 -12.60 REMARK 500 1 GLU A 36 -11.62 REMARK 500 1 ALA A 41 -10.46 REMARK 500 1 ALA A 43 -10.21 REMARK 500 2 VAL A 9 -10.12 REMARK 500 2 ARG A 35 -12.97 REMARK 500 2 GLU A 36 -11.88 REMARK 500 2 ALA A 43 -10.80 REMARK 500 2 ILE A 48 10.09 REMARK 500 3 VAL A 15 11.62 REMARK 500 3 LYS A 33 -10.14 REMARK 500 3 ARG A 35 -11.91 REMARK 500 3 GLU A 36 -12.18 REMARK 500 3 ALA A 41 -10.75 REMARK 500 3 TYR A 47 -10.41 REMARK 500 3 PRO A 49 10.71 REMARK 500 4 VAL A 15 10.10 REMARK 500 4 GLN A 18 -12.24 REMARK 500 4 SER A 21 -11.27 REMARK 500 4 GLN A 26 -11.02 REMARK 500 4 LYS A 33 -11.10 REMARK 500 4 GLU A 36 -11.63 REMARK 500 4 LYS A 37 -12.20 REMARK 500 4 ALA A 43 -10.15 REMARK 500 4 GLN A 55 10.90 REMARK 500 5 ARG A 35 -12.94 REMARK 500 5 GLU A 36 -11.75 REMARK 500 5 ALA A 40 -10.63 REMARK 500 5 ASN A 46 -11.59 REMARK 500 5 GLN A 54 -11.93 REMARK 500 5 GLN A 55 13.10 REMARK 500 6 ARG A 35 -13.77 REMARK 500 6 GLU A 36 -11.15 REMARK 500 6 ALA A 43 -10.32 REMARK 500 6 GLN A 54 -10.01 REMARK 500 7 GLU A 36 -11.78 REMARK 500 7 LYS A 37 -10.08 REMARK 500 8 GLN A 18 -12.75 REMARK 500 8 VAL A 20 -10.92 REMARK 500 8 SER A 21 -11.04 REMARK 500 8 ARG A 35 -11.87 REMARK 500 8 GLU A 36 -10.50 REMARK 500 8 PRO A 49 -10.77 REMARK 500 8 ASN A 50 11.91 REMARK 500 9 GLU A 36 -10.46 REMARK 500 9 LYS A 37 -11.26 REMARK 500 10 GLN A 18 -13.30 REMARK 500 10 SER A 21 -11.13 REMARK 500 REMARK 500 THIS ENTRY HAS 184 MAIN CHAIN PLANARITY DEVIATIONS. REMARK 500 REMARK 500 REMARK: NULL DBREF 1LQC A 1 56 UNP P03023 LACI_ECOLI 1 56 SEQRES 1 A 56 MET LYS PRO VAL THR LEU TYR ASP VAL ALA GLU TYR ALA SEQRES 2 A 56 GLY VAL SER TYR GLN THR VAL SER ARG VAL VAL ASN GLN SEQRES 3 A 56 ALA SER HIS VAL SER ALA LYS THR ARG GLU LYS VAL GLU SEQRES 4 A 56 ALA ALA MET ALA GLU LEU ASN TYR ILE PRO ASN ARG VAL SEQRES 5 A 56 ALA GLN GLN LEU HELIX 1 H1 LEU A 6 ALA A 13 1 8 HELIX 2 H2 TYR A 17 VAL A 24 1 8 HELIX 3 H3 ALA A 32 LEU A 45 1 14 CISPEP 1 ARG A 51 VAL A 52 24 1.59 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 23 2 Bytes