Header list of 1e2b.pdb file
Complete list - v 3 2 Bytes
HEADER TRANSFERASE 15-NOV-96 1E2B TITLE NMR STRUCTURE OF THE C10S MUTANT OF ENZYME IIB CELLOBIOSE OF THE TITLE 2 PHOSPHOENOL-PYRUVATE DEPENDENT PHOSPHOTRANSFERASE SYSTEM OF TITLE 3 ESCHERICHIA COLI, 17 STRUCTURES COMPND MOL_ID: 1; COMPND 2 MOLECULE: ENZYME IIB-CELLOBIOSE; COMPND 3 CHAIN: A; COMPND 4 EC: 2.7.1.69; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI; SOURCE 3 ORGANISM_TAXID: 83333; SOURCE 4 STRAIN: K12; SOURCE 5 CELLULAR_LOCATION: CYTOPLASM; SOURCE 6 GENE: CELA; SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI STR. K12 SUBSTR. W3110; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 316407; SOURCE 9 EXPRESSION_SYSTEM_STRAIN: W3110; SOURCE 10 EXPRESSION_SYSTEM_CELLULAR_LOCATION: CYTOPLASM; SOURCE 11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 12 EXPRESSION_SYSTEM_PLASMID: PJR-IIBC10S KEYWDS ENZYME IIB-CELLOBIOSE, PHOSPHOTRANSFERASE SYSTEM, TRANSFERASE, SUGAR KEYWDS 2 TRANSPORT, PHOSPHORYLATION EXPDTA SOLUTION NMR NUMMDL 17 AUTHOR E.AB,G.SCHUURMAN-WOLTERS,J.REIZER,M.H.SAIER,K.DIJKSTRA,R.M.SCHEEK, AUTHOR 2 G.T.ROBILLARD REVDAT 4 03-NOV-21 1E2B 1 SEQADV REVDAT 3 13-JUL-11 1E2B 1 VERSN REVDAT 2 24-FEB-09 1E2B 1 VERSN REVDAT 1 23-JUL-97 1E2B 0 JRNL AUTH E.AB,G.SCHUURMAN-WOLTERS,J.REIZER,M.H.SAIER,K.DIJKSTRA, JRNL AUTH 2 R.M.SCHEEK,G.T.ROBILLARD JRNL TITL THE NMR SIDE-CHAIN ASSIGNMENTS AND SOLUTION STRUCTURE OF JRNL TITL 2 ENZYME IIBCELLOBIOSE OF THE PHOSPHOENOLPYRUVATE-DEPENDENT JRNL TITL 3 PHOSPHOTRANSFERASE SYSTEM OF ESCHERICHIA COLI. JRNL REF PROTEIN SCI. V. 6 304 1997 JRNL REFN ISSN 0961-8368 JRNL PMID 9041631 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH E.AB,G.K.SCHUURMAN-WOLTERS,M.H.SAIER,J.REIZER,M.JACUINOD, REMARK 1 AUTH 2 P.ROEPSTORFF,K.DIJKSTRA,R.M.SCHEEK,G.T.ROBILLARD REMARK 1 TITL ENZYME IIBCELLOBIOSE OF THE PHOSPHOENOL-PYRUVATE-DEPENDENT REMARK 1 TITL 2 PHOSPHOTRANSFERASE SYSTEM OF ESCHERICHIA COLI: BACKBONE REMARK 1 TITL 3 ASSIGNMENT AND SECONDARY STRUCTURE DETERMINED BY REMARK 1 TITL 4 THREE-DIMENSIONAL NMR SPECTROSCOPY REMARK 1 REF PROTEIN SCI. V. 3 282 1994 REMARK 1 REFN ISSN 0961-8368 REMARK 1 REFERENCE 2 REMARK 1 AUTH L.L.PARKER,B.G.HALL REMARK 1 TITL CHARACTERIZATION AND NUCLEOTIDE SEQUENCE OF THE CRYPTIC CEL REMARK 1 TITL 2 OPERON OF ESCHERICHIA COLI K12 REMARK 1 REF GENETICS V. 124 455 1990 REMARK 1 REFN ISSN 0016-6731 REMARK 1 REFERENCE 3 REMARK 1 AUTH J.REIZER,A.REIZER,M.H.SAIER JUNIOR REMARK 1 TITL THE CELLOBIOSE PERMEASE OF ESCHERICHIA COLI CONSISTS OF REMARK 1 TITL 2 THREE PROTEINS AND IS HOMOLOGOUS TO THE LACTOSE PERMEASE OF REMARK 1 TITL 3 STAPHYLOCOCCUS AUREUS REMARK 1 REF RES.MICROBIOL. V. 141 1061 1990 REMARK 1 REFN ISSN 0923-2508 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : DDD REMARK 3 AUTHORS : SCHEEK REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1E2B 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_1000172975. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 293 REMARK 210 PH : 6.18 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 750 MHZ REMARK 210 SPECTROMETER MODEL : UNITY REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : SNARF, DDD REMARK 210 METHOD USED : DISTANCE GEOMETRY, RESTRAINED REMARK 210 MOLECULAR DYNAMICS, SIMULATED REMARK 210 ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 32 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 17 REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION, NUMBER OF REMARK 210 VIOLATIONS 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 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 ALA A 25 H LYS A 29 1.50 REMARK 500 O LEU A 43 H LYS A 47 1.53 REMARK 500 O GLY A 91 HB1 ALA A 95 1.54 REMARK 500 O ASP A 80 HB2 TYR A 84 1.54 REMARK 500 O MET A 63 H ILE A 67 1.55 REMARK 500 OE1 GLN A 26 HD11 LEU A 90 1.57 REMARK 500 O PHE A 9 H GLY A 57 1.57 REMARK 500 O TYR A 84 H VAL A 87 1.57 REMARK 500 O LEU A 8 H PHE A 39 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 3 GLU A 31 CD GLU A 31 OE2 0.082 REMARK 500 4 PHE A 39 CA PHE A 39 CB 0.133 REMARK 500 7 GLU A 37 CD GLU A 37 OE1 0.067 REMARK 500 17 VAL A 34 CB VAL A 34 CG1 0.140 REMARK 500 17 GLU A 41 CD GLU A 41 OE2 0.073 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 7 CB - CG - CD2 ANGL. DEV. = -3.9 DEGREES REMARK 500 1 TYR A 84 CB - CG - CD2 ANGL. DEV. = -3.6 DEGREES REMARK 500 2 GLN A 26 CA - CB - CG ANGL. DEV. = 15.6 DEGREES REMARK 500 2 TYR A 84 CB - CG - CD2 ANGL. DEV. = -3.8 DEGREES REMARK 500 3 PHE A 9 CB - CG - CD1 ANGL. DEV. = -4.4 DEGREES REMARK 500 3 TYR A 30 CB - CG - CD1 ANGL. DEV. = -4.4 DEGREES REMARK 500 4 TYR A 7 CB - CG - CD2 ANGL. DEV. = -4.7 DEGREES REMARK 500 4 THR A 16 N - CA - CB ANGL. DEV. = 13.1 DEGREES REMARK 500 4 ARG A 24 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES REMARK 500 4 TYR A 30 CB - CG - CD1 ANGL. DEV. = -4.4 DEGREES REMARK 500 4 TYR A 62 CB - CG - CD2 ANGL. DEV. = -3.9 DEGREES REMARK 500 5 TYR A 7 CB - CG - CD2 ANGL. DEV. = -4.6 DEGREES REMARK 500 5 TYR A 30 CB - CG - CD2 ANGL. DEV. = -4.0 DEGREES REMARK 500 6 TYR A 7 CB - CG - CD2 ANGL. DEV. = -4.1 DEGREES REMARK 500 6 PRO A 33 C - N - CA ANGL. DEV. = 11.0 DEGREES REMARK 500 7 GLN A 26 CA - CB - CG ANGL. DEV. = 14.8 DEGREES REMARK 500 7 TYR A 62 CB - CG - CD2 ANGL. DEV. = -4.3 DEGREES REMARK 500 8 TYR A 7 CB - CG - CD2 ANGL. DEV. = -3.8 DEGREES REMARK 500 8 TYR A 30 CB - CG - CD1 ANGL. DEV. = -4.5 DEGREES REMARK 500 8 PRO A 40 C - N - CA ANGL. DEV. = 10.0 DEGREES REMARK 500 9 LEU A 8 N - CA - CB ANGL. DEV. = -13.2 DEGREES REMARK 500 9 TYR A 30 CB - CG - CD1 ANGL. DEV. = -3.7 DEGREES REMARK 500 9 TYR A 62 CB - CG - CD2 ANGL. DEV. = -4.4 DEGREES REMARK 500 9 PRO A 72 C - N - CA ANGL. DEV. = 9.1 DEGREES REMARK 500 10 TYR A 7 CB - CG - CD1 ANGL. DEV. = -4.3 DEGREES REMARK 500 10 TYR A 30 CB - CG - CD2 ANGL. DEV. = -4.1 DEGREES REMARK 500 10 TYR A 62 CB - CG - CD2 ANGL. DEV. = -4.4 DEGREES REMARK 500 11 LEU A 8 N - CA - CB ANGL. DEV. = -12.6 DEGREES REMARK 500 11 ARG A 24 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES REMARK 500 11 ARG A 69 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES REMARK 500 11 TYR A 84 CB - CG - CD2 ANGL. DEV. = -3.8 DEGREES REMARK 500 12 TYR A 30 CB - CG - CD1 ANGL. DEV. = -3.9 DEGREES REMARK 500 12 PRO A 40 C - N - CA ANGL. DEV. = 9.5 DEGREES REMARK 500 12 TYR A 62 CB - CG - CD2 ANGL. DEV. = -4.2 DEGREES REMARK 500 12 ARG A 69 NE - CZ - NH2 ANGL. DEV. = 3.1 DEGREES REMARK 500 12 TYR A 84 CB - CG - CD2 ANGL. DEV. = -4.0 DEGREES REMARK 500 13 TYR A 30 CB - CG - CD1 ANGL. DEV. = -4.7 DEGREES REMARK 500 14 TYR A 7 CB - CG - CD2 ANGL. DEV. = -3.7 DEGREES REMARK 500 14 TYR A 30 CB - CG - CD1 ANGL. DEV. = -4.0 DEGREES REMARK 500 14 TYR A 62 CB - CG - CD2 ANGL. DEV. = -4.5 DEGREES REMARK 500 15 TYR A 62 CB - CG - CD2 ANGL. DEV. = -3.7 DEGREES REMARK 500 16 LEU A 8 N - CA - CB ANGL. DEV. = -13.8 DEGREES REMARK 500 16 TYR A 30 CB - CG - CD1 ANGL. DEV. = -4.1 DEGREES REMARK 500 16 TYR A 62 CB - CG - CD2 ANGL. DEV. = -4.9 DEGREES REMARK 500 17 TYR A 7 CB - CG - CD2 ANGL. DEV. = -3.7 DEGREES REMARK 500 17 LEU A 8 CA - CB - CG ANGL. DEV. = 14.0 DEGREES REMARK 500 17 ARG A 24 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES REMARK 500 17 TYR A 30 CB - CG - CD1 ANGL. DEV. = -4.8 DEGREES REMARK 500 17 ILE A 35 CG1 - CB - CG2 ANGL. DEV. = 13.7 DEGREES REMARK 500 17 VAL A 87 CA - CB - CG1 ANGL. DEV. = 9.5 DEGREES 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 2 3.17 82.68 REMARK 500 1 LYS A 3 149.03 -171.03 REMARK 500 1 THR A 16 -59.33 -136.69 REMARK 500 1 ALA A 25 -73.22 -30.81 REMARK 500 1 GLN A 26 -80.67 -18.59 REMARK 500 1 TYR A 30 -137.48 -123.48 REMARK 500 1 VAL A 32 117.37 -34.40 REMARK 500 1 GLU A 41 19.84 27.37 REMARK 500 1 ALA A 61 -44.38 -22.48 REMARK 500 1 ARG A 69 -70.21 -72.13 REMARK 500 1 LEU A 70 -45.77 -27.79 REMARK 500 1 PRO A 72 46.95 -92.32 REMARK 500 1 ASN A 73 -56.86 -161.21 REMARK 500 1 LYS A 74 158.31 -42.80 REMARK 500 1 PRO A 75 49.53 -81.92 REMARK 500 1 GLU A 77 114.41 -163.93 REMARK 500 1 TYR A 84 -83.39 -47.71 REMARK 500 1 ASP A 88 65.36 -101.99 REMARK 500 1 LEU A 90 -36.19 -144.69 REMARK 500 1 ALA A 105 71.64 153.81 REMARK 500 2 SER A 10 -159.00 40.91 REMARK 500 2 SER A 11 -54.75 145.67 REMARK 500 2 ALA A 12 25.77 -144.12 REMARK 500 2 MET A 14 30.76 99.73 REMARK 500 2 VAL A 20 -80.13 -34.91 REMARK 500 2 MET A 23 -74.20 -39.60 REMARK 500 2 ARG A 24 -36.95 -35.06 REMARK 500 2 GLN A 26 -66.89 -25.06 REMARK 500 2 GLU A 31 10.58 82.84 REMARK 500 2 GLU A 41 -55.34 -19.25 REMARK 500 2 THR A 42 -53.36 -4.90 REMARK 500 2 VAL A 53 89.11 -167.50 REMARK 500 2 ALA A 61 -53.11 -20.04 REMARK 500 2 LEU A 71 73.01 -119.12 REMARK 500 2 TYR A 84 -79.26 -46.45 REMARK 500 2 VAL A 87 85.31 75.61 REMARK 500 2 LEU A 90 -38.34 176.99 REMARK 500 2 ALA A 104 -165.26 -166.40 REMARK 500 2 ALA A 105 -62.76 106.41 REMARK 500 3 GLU A 2 -64.76 -140.96 REMARK 500 3 LYS A 3 141.02 168.44 REMARK 500 3 SER A 11 -60.20 -154.85 REMARK 500 3 THR A 16 -73.76 -44.48 REMARK 500 3 GLU A 31 8.97 102.24 REMARK 500 3 PRO A 33 93.89 -63.16 REMARK 500 3 VAL A 34 141.31 -177.68 REMARK 500 3 GLU A 41 -50.68 46.93 REMARK 500 3 THR A 42 -37.37 -23.75 REMARK 500 3 PRO A 75 69.80 -34.78 REMARK 500 3 GLU A 77 134.71 179.91 REMARK 500 REMARK 500 THIS ENTRY HAS 333 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 PHE A 9 SER A 10 1 -146.74 REMARK 500 GLU A 28 LYS A 29 1 148.63 REMARK 500 MET A 14 SER A 15 2 144.28 REMARK 500 MET A 14 SER A 15 3 147.69 REMARK 500 MET A 14 SER A 15 4 148.15 REMARK 500 PHE A 9 SER A 10 5 -148.69 REMARK 500 PHE A 9 SER A 10 6 -145.21 REMARK 500 MET A 14 SER A 15 6 147.85 REMARK 500 PRO A 33 VAL A 34 6 -148.07 REMARK 500 ILE A 35 ILE A 36 6 145.81 REMARK 500 ALA A 51 ASP A 52 6 149.73 REMARK 500 LEU A 70 LEU A 71 6 148.29 REMARK 500 PHE A 9 SER A 10 7 -145.67 REMARK 500 SER A 10 SER A 11 8 146.91 REMARK 500 MET A 14 SER A 15 8 146.45 REMARK 500 LEU A 18 LEU A 19 9 149.98 REMARK 500 VAL A 34 ILE A 35 9 149.67 REMARK 500 HIS A 5 ILE A 6 10 142.41 REMARK 500 MET A 14 SER A 15 10 -149.79 REMARK 500 GLN A 59 ILE A 60 10 144.19 REMARK 500 PHE A 9 SER A 10 12 -147.71 REMARK 500 ALA A 51 ASP A 52 12 149.28 REMARK 500 PHE A 9 SER A 10 14 -149.33 REMARK 500 LEU A 8 PHE A 9 15 -146.62 REMARK 500 PRO A 58 GLN A 59 15 145.71 REMARK 500 MET A 14 SER A 15 16 149.90 REMARK 500 ILE A 35 ILE A 36 16 144.62 REMARK 500 ILE A 35 ILE A 36 17 147.28 REMARK 500 THR A 42 LEU A 43 17 -149.65 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 7 0.09 SIDE CHAIN REMARK 500 1 TYR A 30 0.09 SIDE CHAIN REMARK 500 1 PHE A 39 0.08 SIDE CHAIN REMARK 500 2 TYR A 7 0.08 SIDE CHAIN REMARK 500 2 TYR A 30 0.07 SIDE CHAIN REMARK 500 2 TYR A 62 0.08 SIDE CHAIN REMARK 500 3 TYR A 7 0.08 SIDE CHAIN REMARK 500 3 TYR A 30 0.07 SIDE CHAIN REMARK 500 3 TYR A 62 0.11 SIDE CHAIN REMARK 500 3 TYR A 84 0.09 SIDE CHAIN REMARK 500 4 PHE A 9 0.10 SIDE CHAIN REMARK 500 4 TYR A 84 0.09 SIDE CHAIN REMARK 500 5 PHE A 9 0.08 SIDE CHAIN REMARK 500 5 TYR A 62 0.08 SIDE CHAIN REMARK 500 5 TYR A 84 0.08 SIDE CHAIN REMARK 500 6 HIS A 5 0.08 SIDE CHAIN REMARK 500 6 TYR A 7 0.11 SIDE CHAIN REMARK 500 6 PHE A 9 0.07 SIDE CHAIN REMARK 500 6 PHE A 39 0.08 SIDE CHAIN REMARK 500 6 TYR A 62 0.13 SIDE CHAIN REMARK 500 6 TYR A 84 0.14 SIDE CHAIN REMARK 500 7 PHE A 9 0.09 SIDE CHAIN REMARK 500 7 PHE A 39 0.07 SIDE CHAIN REMARK 500 8 HIS A 5 0.09 SIDE CHAIN REMARK 500 8 PHE A 39 0.10 SIDE CHAIN REMARK 500 8 TYR A 62 0.12 SIDE CHAIN REMARK 500 8 TYR A 84 0.10 SIDE CHAIN REMARK 500 9 TYR A 7 0.11 SIDE CHAIN REMARK 500 9 PHE A 9 0.09 SIDE CHAIN REMARK 500 9 TYR A 30 0.08 SIDE CHAIN REMARK 500 9 TYR A 62 0.08 SIDE CHAIN REMARK 500 9 TYR A 84 0.10 SIDE CHAIN REMARK 500 10 TYR A 7 0.09 SIDE CHAIN REMARK 500 10 TYR A 62 0.16 SIDE CHAIN REMARK 500 11 PHE A 9 0.10 SIDE CHAIN REMARK 500 11 PHE A 39 0.08 SIDE CHAIN REMARK 500 11 TYR A 62 0.09 SIDE CHAIN REMARK 500 11 TYR A 84 0.09 SIDE CHAIN REMARK 500 12 TYR A 7 0.11 SIDE CHAIN REMARK 500 12 PHE A 9 0.11 SIDE CHAIN REMARK 500 12 TYR A 30 0.08 SIDE CHAIN REMARK 500 12 PHE A 39 0.09 SIDE CHAIN REMARK 500 12 TYR A 62 0.08 SIDE CHAIN REMARK 500 13 PHE A 9 0.07 SIDE CHAIN REMARK 500 13 TYR A 84 0.07 SIDE CHAIN REMARK 500 14 PHE A 9 0.08 SIDE CHAIN REMARK 500 14 TYR A 30 0.08 SIDE CHAIN REMARK 500 14 TYR A 62 0.11 SIDE CHAIN REMARK 500 15 TYR A 62 0.09 SIDE CHAIN REMARK 500 15 TYR A 84 0.08 SIDE CHAIN REMARK 500 REMARK 500 THIS ENTRY HAS 58 PLANE DEVIATIONS. REMARK 500 REMARK 500 REMARK: NULL DBREF 1E2B A 1 106 UNP P69795 PTQB_ECOLI 1 106 SEQADV 1E2B SER A 10 UNP P69795 CYS 10 ENGINEERED MUTATION SEQRES 1 A 106 MET GLU LYS LYS HIS ILE TYR LEU PHE SER SER ALA GLY SEQRES 2 A 106 MET SER THR SER LEU LEU VAL SER LYS MET ARG ALA GLN SEQRES 3 A 106 ALA GLU LYS TYR GLU VAL PRO VAL ILE ILE GLU ALA PHE SEQRES 4 A 106 PRO GLU THR LEU ALA GLY GLU LYS GLY GLN ASN ALA ASP SEQRES 5 A 106 VAL VAL LEU LEU GLY PRO GLN ILE ALA TYR MET LEU PRO SEQRES 6 A 106 GLU ILE GLN ARG LEU LEU PRO ASN LYS PRO VAL GLU VAL SEQRES 7 A 106 ILE ASP SER LEU LEU TYR GLY LYS VAL ASP GLY LEU GLY SEQRES 8 A 106 VAL LEU LYS ALA ALA VAL ALA ALA ILE LYS LYS ALA ALA SEQRES 9 A 106 ALA ASN HELIX 1 H1 THR A 16 LYS A 29 1 14 HELIX 2 H2 LEU A 43 ALA A 51 1 9 HELIX 3 H3 MET A 63 LEU A 70 1 8 HELIX 4 H4 ASP A 80 VAL A 87 1 8 HELIX 5 H5 LEU A 90 ALA A 103 1 14 SHEET 1 S1 4 VAL A 34 PHE A 39 0 SHEET 2 S1 4 LYS A 4 SER A 10 1 N LEU A 8 O GLU A 37 SHEET 3 S1 4 VAL A 53 GLY A 57 1 N LEU A 55 O TYR A 7 SHEET 4 S1 4 VAL A 76 ILE A 79 1 N GLU A 77 O VAL A 54 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 3 2 Bytes