Header list of 2ife.pdb file
Complete list - r 9 2 Bytes
HEADER GENE REGULATION 16-DEC-98 2IFE TITLE TRANSLATION INITIATION FACTOR IF3 FROM ESCHERICHIA COLI RIBOSOME TITLE 2 BINDING DOMAIN (RESIDUES 84-180) COMPND MOL_ID: 1; COMPND 2 MOLECULE: PROTEIN (TRANSLATION INITIATION FACTOR IF3); COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: RIBOSOME-BINDING DOMAIN; COMPND 5 ENGINEERED: YES; COMPND 6 OTHER_DETAILS: PRODUCT OF THE INFC GENE SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI; SOURCE 3 ORGANISM_TAXID: 562; SOURCE 4 STRAIN: JM83; SOURCE 5 GENE: INFC CODONS 84-180; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: JM83; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_VECTOR: PTRC99A; SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PTRCINFCC; SOURCE 12 EXPRESSION_SYSTEM_GENE: INFC CODONS 84-180 KEYWDS INITIATION FACTOR, GENE REGULATION EXPDTA SOLUTION NMR NUMMDL 24 AUTHOR E.DE COCK,C.GARCIA,F.DARDEL REVDAT 5 09-MAR-22 2IFE 1 REMARK REVDAT 4 24-FEB-09 2IFE 1 VERSN REVDAT 3 16-AUG-00 2IFE 1 COMPND REMARK REVDAT 2 29-DEC-99 2IFE 4 HEADER COMPND REMARK JRNL REVDAT 2 2 4 ATOM SOURCE SEQRES REVDAT 1 23-DEC-98 2IFE 0 SPRSDE 23-DEC-98 2IFE 1IFE JRNL AUTH E.DE COCK,S.BLANQUET,J.-Y.LALLEMAND,F.DARDEL JRNL TITL INTERACTION OF E. COLI TRANSLATION INITIATION FACTOR IF3 JRNL TITL 2 WITH THE RIBOSOME JRNL REF TO BE PUBLISHED JRNL REFN REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH C.GARCIA,P.-L.FORTIER,S.BLANQUET,J.-Y.LALLEMAND,F.DARDEL REMARK 1 TITL SOLUTION STRUCTURE OF THE RIBOSOME-BINDING DOMAIN OF E. COLI REMARK 1 TITL 2 TRANSLATION INITIATION FACTOR IF3. HOMOLOGY WITH THE U1A REMARK 1 TITL 3 PROTEIN OF THE EUKARYOTIC SPLICEOSOME REMARK 1 REF J.MOL.BIOL. V. 254 247 1995 REMARK 1 REFN ISSN 0022-2836 REMARK 1 REFERENCE 2 REMARK 1 AUTH C.GARCIA,P.-L.FORTIER,S.BLANQUET,J.-Y.LALLEMAND,F.DARDEL REMARK 1 TITL 1H AND 15N RESONANCE ASSIGNMENT AND STRUCTURE OF N-TERMINAL REMARK 1 TITL 2 DOMAIN OF ESCHERICHIA COLI INITIATION FACTOR 3 REMARK 1 REF EUR.J.BIOCHEM. V. 228 395 1995 REMARK 1 REFN ISSN 0014-2956 REMARK 1 REFERENCE 3 REMARK 1 AUTH P.-L.FORTIER,J.-M.SCHMITTER,C.GARCIA,F.DARDEL REMARK 1 TITL THE N-TERMINAL OF INITIATION FACTOR IF3 IS FOLDED AS A REMARK 1 TITL 2 STABLE INDEPENDENT DOMAIN REMARK 1 REF BIOCHIMIE V. 76 376 1994 REMARK 1 REFN ISSN 0300-9084 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: REFINEMENT DETAILS CAN BE FOUND IN THE REMARK 3 JRNL CITATION REMARK 4 REMARK 4 2IFE COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB. REMARK 100 THE DEPOSITION ID IS D_1000008034. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 303 REMARK 210 PH : 6.5 REMARK 210 IONIC STRENGTH : 20 MM POTASSIUM PHOSPHATE REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : HMQC-NOESY; HCCH-TOCSY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : DRX600 REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : DIANA, X-PLOR 3.1 REMARK 210 METHOD USED : DISTANCE GEOMETRY AND RESTRAINED REMARK 210 SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 200 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 24 REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST TARGET FUNCTION REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 2 REMARK 210 REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR REMARK 210 SPECTROSCOPY ON A 13C, 15N-LABELLED SAMPLE 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 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 1-24 REMARK 465 RES C SSSEQI REMARK 465 MET A 81 REMARK 465 GLU A 82 REMARK 465 PHE A 83 REMARK 465 GLN A 84 REMARK 465 LYS A 85 REMARK 465 LYS A 86 REMARK 465 LYS A 87 REMARK 465 GLN A 88 REMARK 465 LYS A 89 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 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 TYR A 107 CB - CG - CD2 ANGL. DEV. = -4.8 DEGREES REMARK 500 1 VAL A 144 CA - CB - CG2 ANGL. DEV. = -11.1 DEGREES REMARK 500 1 LEU A 152 CB - CA - C ANGL. DEV. = -11.6 DEGREES REMARK 500 1 ALA A 156 CB - CA - C ANGL. DEV. = -10.3 DEGREES REMARK 500 2 LEU A 114 N - CA - CB ANGL. DEV. = -12.1 DEGREES REMARK 500 2 PHE A 117 CB - CG - CD2 ANGL. DEV. = -8.6 DEGREES REMARK 500 2 PHE A 117 CB - CG - CD1 ANGL. DEV. = 6.8 DEGREES REMARK 500 2 VAL A 144 CA - CB - CG2 ANGL. DEV. = -10.7 DEGREES REMARK 500 2 ALA A 156 CB - CA - C ANGL. DEV. = -12.0 DEGREES REMARK 500 2 PHE A 161 CB - CG - CD1 ANGL. DEV. = -5.1 DEGREES REMARK 500 3 VAL A 144 CA - CB - CG2 ANGL. DEV. = -10.7 DEGREES REMARK 500 3 LEU A 152 CB - CA - C ANGL. DEV. = -11.7 DEGREES REMARK 500 3 ALA A 156 CB - CA - C ANGL. DEV. = -11.0 DEGREES REMARK 500 3 PHE A 161 CB - CG - CD1 ANGL. DEV. = -5.0 DEGREES REMARK 500 4 VAL A 144 CA - CB - CG2 ANGL. DEV. = -10.9 DEGREES REMARK 500 4 ALA A 156 CB - CA - C ANGL. DEV. = -10.0 DEGREES REMARK 500 5 VAL A 93 CG1 - CB - CG2 ANGL. DEV. = -9.7 DEGREES REMARK 500 5 PHE A 98 CB - CG - CD2 ANGL. DEV. = -9.1 DEGREES REMARK 500 5 PHE A 98 CB - CG - CD1 ANGL. DEV. = 8.6 DEGREES REMARK 500 5 THR A 102 CA - CB - CG2 ANGL. DEV. = -8.4 DEGREES REMARK 500 5 TYR A 107 CB - CG - CD2 ANGL. DEV. = -3.7 DEGREES REMARK 500 5 PHE A 117 CB - CG - CD2 ANGL. DEV. = -8.6 DEGREES REMARK 500 5 PHE A 117 CB - CG - CD1 ANGL. DEV. = 7.8 DEGREES REMARK 500 5 VAL A 144 CA - CB - CG2 ANGL. DEV. = -10.6 DEGREES REMARK 500 5 ALA A 156 CB - CA - C ANGL. DEV. = -12.7 DEGREES REMARK 500 5 ALA A 175 CB - CA - C ANGL. DEV. = -10.4 DEGREES REMARK 500 6 TYR A 107 CB - CG - CD2 ANGL. DEV. = -4.2 DEGREES REMARK 500 6 VAL A 144 CA - CB - CG2 ANGL. DEV. = -11.7 DEGREES REMARK 500 6 LEU A 152 CB - CA - C ANGL. DEV. = -12.0 DEGREES REMARK 500 6 ALA A 156 CB - CA - C ANGL. DEV. = -12.4 DEGREES REMARK 500 6 ALA A 156 N - CA - CB ANGL. DEV. = 9.2 DEGREES REMARK 500 6 THR A 163 N - CA - CB ANGL. DEV. = -12.4 DEGREES REMARK 500 7 VAL A 144 CA - CB - CG2 ANGL. DEV. = -11.4 DEGREES REMARK 500 7 LEU A 152 CB - CA - C ANGL. DEV. = -13.0 DEGREES REMARK 500 7 ALA A 156 CB - CA - C ANGL. DEV. = -11.3 DEGREES REMARK 500 7 ALA A 156 N - CA - CB ANGL. DEV. = 9.1 DEGREES REMARK 500 7 ALA A 175 CB - CA - C ANGL. DEV. = -11.1 DEGREES REMARK 500 8 PHE A 117 CB - CG - CD2 ANGL. DEV. = -8.8 DEGREES REMARK 500 8 PHE A 117 CB - CG - CD1 ANGL. DEV. = 7.1 DEGREES REMARK 500 8 VAL A 144 CA - CB - CG2 ANGL. DEV. = -10.4 DEGREES REMARK 500 8 ALA A 156 CB - CA - C ANGL. DEV. = -10.6 DEGREES REMARK 500 8 ALA A 156 N - CA - CB ANGL. DEV. = 9.2 DEGREES REMARK 500 9 TYR A 107 CB - CG - CD2 ANGL. DEV. = -4.0 DEGREES REMARK 500 9 VAL A 144 CA - CB - CG2 ANGL. DEV. = -11.3 DEGREES REMARK 500 9 LEU A 152 CB - CA - C ANGL. DEV. = -11.5 DEGREES REMARK 500 9 ALA A 156 CB - CA - C ANGL. DEV. = -10.9 DEGREES REMARK 500 9 PHE A 161 CB - CG - CD1 ANGL. DEV. = -5.8 DEGREES REMARK 500 10 PHE A 98 CB - CG - CD2 ANGL. DEV. = -8.0 DEGREES REMARK 500 10 PHE A 98 CB - CG - CD1 ANGL. DEV. = 7.9 DEGREES REMARK 500 10 TYR A 107 CB - CG - CD2 ANGL. DEV. = -8.4 DEGREES REMARK 500 REMARK 500 THIS ENTRY HAS 145 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 GLU A 104 -56.21 -27.32 REMARK 500 1 TYR A 107 -71.17 -73.95 REMARK 500 1 GLN A 139 -57.41 -120.84 REMARK 500 1 GLN A 153 -27.04 -26.38 REMARK 500 1 THR A 163 50.41 8.22 REMARK 500 1 ARG A 168 33.83 -95.54 REMARK 500 2 ASP A 103 -150.55 -133.85 REMARK 500 2 TYR A 107 -73.71 -66.91 REMARK 500 2 MET A 135 -100.57 -61.81 REMARK 500 2 ALA A 136 112.30 171.27 REMARK 500 2 GLN A 153 -27.96 -27.51 REMARK 500 2 PRO A 162 -91.32 -83.79 REMARK 500 2 THR A 163 -104.58 -132.49 REMARK 500 3 TYR A 107 -73.29 -85.70 REMARK 500 3 ARG A 133 -179.85 61.04 REMARK 500 3 GLU A 134 99.05 3.83 REMARK 500 3 MET A 135 73.71 55.58 REMARK 500 3 ALA A 136 -143.52 -81.27 REMARK 500 3 GLN A 153 -25.78 -28.42 REMARK 500 3 PRO A 162 -119.00 -133.20 REMARK 500 3 THR A 163 -40.92 -170.40 REMARK 500 3 ARG A 168 44.83 -108.90 REMARK 500 4 GLU A 104 -57.16 -24.00 REMARK 500 4 TYR A 107 -72.58 -72.83 REMARK 500 4 ARG A 133 101.70 -29.74 REMARK 500 4 GLU A 134 -110.18 -114.88 REMARK 500 4 ALA A 136 -151.29 -80.65 REMARK 500 4 GLU A 143 -71.65 -54.74 REMARK 500 4 GLN A 153 -26.94 -28.26 REMARK 500 4 PRO A 162 -116.65 -107.44 REMARK 500 4 THR A 163 -48.47 175.28 REMARK 500 4 GLN A 169 130.93 -172.13 REMARK 500 4 LYS A 178 79.63 -100.96 REMARK 500 5 TYR A 107 -72.18 -87.14 REMARK 500 5 ARG A 131 -76.75 -57.54 REMARK 500 5 HIS A 137 120.31 -22.05 REMARK 500 5 GLN A 153 -22.31 -28.07 REMARK 500 5 LEU A 155 -52.77 -121.60 REMARK 500 5 PRO A 162 -118.23 -132.69 REMARK 500 5 THR A 163 -44.20 -174.22 REMARK 500 5 ARG A 168 38.14 -96.46 REMARK 500 5 LEU A 174 69.12 -105.20 REMARK 500 6 THR A 102 103.82 52.34 REMARK 500 6 ASP A 103 -139.44 -131.39 REMARK 500 6 GLU A 104 -72.76 -62.06 REMARK 500 6 TYR A 107 -71.78 -73.90 REMARK 500 6 HIS A 137 -95.75 0.43 REMARK 500 6 GLN A 153 -23.79 -26.24 REMARK 500 6 THR A 163 48.78 9.66 REMARK 500 7 THR A 102 119.08 -163.63 REMARK 500 REMARK 500 THIS ENTRY HAS 226 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 ASP A 103 GLU A 104 1 -145.82 REMARK 500 HIS A 137 GLN A 138 1 149.60 REMARK 500 ALA A 156 VAL A 157 1 139.68 REMARK 500 PHE A 161 PRO A 162 1 -148.65 REMARK 500 ASP A 103 GLU A 104 2 -85.25 REMARK 500 MET A 135 ALA A 136 2 -145.90 REMARK 500 MET A 142 GLU A 143 2 133.87 REMARK 500 PHE A 161 PRO A 162 2 -130.19 REMARK 500 PRO A 162 THR A 163 2 -144.18 REMARK 500 ASP A 103 GLU A 104 3 -132.35 REMARK 500 MET A 142 GLU A 143 3 135.23 REMARK 500 PRO A 162 THR A 163 3 -128.69 REMARK 500 ASP A 103 GLU A 104 4 -149.66 REMARK 500 ARG A 133 GLU A 134 4 148.79 REMARK 500 GLU A 134 MET A 135 4 148.62 REMARK 500 MET A 142 GLU A 143 4 138.33 REMARK 500 ALA A 156 VAL A 157 4 134.74 REMARK 500 PRO A 162 THR A 163 4 -140.44 REMARK 500 ASP A 103 GLU A 104 5 -138.60 REMARK 500 ARG A 131 GLY A 132 5 148.86 REMARK 500 ALA A 136 HIS A 137 5 147.67 REMARK 500 ALA A 156 VAL A 157 5 147.65 REMARK 500 PRO A 162 THR A 163 5 -133.09 REMARK 500 ASP A 103 GLU A 104 6 -84.83 REMARK 500 GLY A 105 ASP A 106 6 147.63 REMARK 500 ARG A 131 GLY A 132 6 -143.61 REMARK 500 ALA A 156 VAL A 157 6 140.63 REMARK 500 SER A 160 PHE A 161 6 139.18 REMARK 500 PHE A 161 PRO A 162 6 -145.73 REMARK 500 ASP A 103 GLU A 104 7 -90.07 REMARK 500 ARG A 131 GLY A 132 7 148.13 REMARK 500 MET A 142 GLU A 143 7 140.40 REMARK 500 ALA A 156 VAL A 157 7 141.31 REMARK 500 PHE A 161 PRO A 162 7 -139.48 REMARK 500 PRO A 162 THR A 163 7 -136.39 REMARK 500 ASP A 103 GLU A 104 8 -84.90 REMARK 500 GLY A 105 ASP A 106 8 148.90 REMARK 500 MET A 142 GLU A 143 8 143.15 REMARK 500 ALA A 156 VAL A 157 8 141.67 REMARK 500 PHE A 161 PRO A 162 8 -137.07 REMARK 500 PRO A 162 THR A 163 8 -139.24 REMARK 500 ASP A 103 GLU A 104 9 -128.82 REMARK 500 MET A 142 GLU A 143 9 137.64 REMARK 500 ALA A 156 VAL A 157 9 148.10 REMARK 500 PHE A 161 PRO A 162 9 -136.56 REMARK 500 PRO A 162 THR A 163 9 -84.86 REMARK 500 THR A 102 ASP A 103 10 -142.97 REMARK 500 GLY A 105 ASP A 106 10 144.26 REMARK 500 MET A 142 GLU A 143 10 129.00 REMARK 500 ALA A 156 VAL A 157 10 141.65 REMARK 500 REMARK 500 THIS ENTRY HAS 128 NON CIS, NON-TRANS OMEGA 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 TYR A 107 0.15 SIDE CHAIN REMARK 500 1 PHE A 161 0.09 SIDE CHAIN REMARK 500 2 TYR A 107 0.14 SIDE CHAIN REMARK 500 2 PHE A 161 0.12 SIDE CHAIN REMARK 500 3 TYR A 107 0.13 SIDE CHAIN REMARK 500 3 PHE A 161 0.16 SIDE CHAIN REMARK 500 4 TYR A 107 0.14 SIDE CHAIN REMARK 500 4 PHE A 161 0.09 SIDE CHAIN REMARK 500 5 TYR A 107 0.17 SIDE CHAIN REMARK 500 5 PHE A 161 0.09 SIDE CHAIN REMARK 500 6 TYR A 107 0.15 SIDE CHAIN REMARK 500 6 PHE A 161 0.10 SIDE CHAIN REMARK 500 7 TYR A 107 0.18 SIDE CHAIN REMARK 500 8 TYR A 107 0.12 SIDE CHAIN REMARK 500 9 TYR A 107 0.17 SIDE CHAIN REMARK 500 10 TYR A 107 0.17 SIDE CHAIN REMARK 500 10 PHE A 161 0.15 SIDE CHAIN REMARK 500 11 TYR A 107 0.14 SIDE CHAIN REMARK 500 12 TYR A 107 0.15 SIDE CHAIN REMARK 500 13 TYR A 107 0.16 SIDE CHAIN REMARK 500 13 PHE A 161 0.13 SIDE CHAIN REMARK 500 14 TYR A 107 0.11 SIDE CHAIN REMARK 500 15 TYR A 107 0.15 SIDE CHAIN REMARK 500 15 PHE A 161 0.15 SIDE CHAIN REMARK 500 16 TYR A 107 0.13 SIDE CHAIN REMARK 500 17 TYR A 107 0.15 SIDE CHAIN REMARK 500 18 TYR A 107 0.16 SIDE CHAIN REMARK 500 19 TYR A 107 0.15 SIDE CHAIN REMARK 500 20 TYR A 107 0.16 SIDE CHAIN REMARK 500 20 PHE A 161 0.11 SIDE CHAIN REMARK 500 21 TYR A 107 0.18 SIDE CHAIN REMARK 500 22 TYR A 107 0.12 SIDE CHAIN REMARK 500 22 PHE A 161 0.08 SIDE CHAIN REMARK 500 23 TYR A 107 0.12 SIDE CHAIN REMARK 500 24 TYR A 107 0.12 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL DBREF 2IFE A 81 180 UNP P0A707 IF3_ECOLI 81 180 SEQADV 2IFE MET A 81 UNP P0A707 SER 81 SEE REMARK 999 SEQADV 2IFE GLU A 82 UNP P0A707 LYS 82 SEE REMARK 999 SEQADV 2IFE PHE A 83 UNP P0A707 GLU 83 SEE REMARK 999 SEQRES 1 A 100 MET GLU PHE GLN LYS LYS LYS GLN LYS VAL ILE GLN VAL SEQRES 2 A 100 LYS GLU ILE LYS PHE ARG PRO GLY THR ASP GLU GLY ASP SEQRES 3 A 100 TYR GLN VAL LYS LEU ARG SER LEU ILE ARG PHE LEU GLU SEQRES 4 A 100 GLU GLY ASP LYS ALA LYS ILE THR LEU ARG PHE ARG GLY SEQRES 5 A 100 ARG GLU MET ALA HIS GLN GLN ILE GLY MET GLU VAL LEU SEQRES 6 A 100 ASN ARG VAL LYS ASP ASP LEU GLN GLU LEU ALA VAL VAL SEQRES 7 A 100 GLU SER PHE PRO THR LYS ILE GLU GLY ARG GLN MET ILE SEQRES 8 A 100 MET VAL LEU ALA PRO LYS LYS LYS GLN HELIX 1 1 GLU A 104 TYR A 107 1 4 HELIX 2 2 VAL A 109 GLU A 119 1 11 HELIX 3 3 ILE A 140 LEU A 152 1 13 SHEET 1 A 3 GLN A 92 ARG A 99 0 SHEET 2 A 3 ASP A 122 ARG A 129 1 N LYS A 123 O GLN A 92 SHEET 3 A 3 GLN A 169 LEU A 174 -1 N LEU A 174 O ALA A 124 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 9 2 Bytes