Header list of 1c3y.pdb file
Complete list - b 16 2 Bytes
HEADER ANTIFREEZE PROTEIN 10-JUL-99 1C3Y TITLE THP12-CARRIER PROTEIN FROM YELLOW MEAL WORM COMPND MOL_ID: 1; COMPND 2 MOLECULE: THP12 CARRIER PROTEIN; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: TENEBRIO MOLITOR; SOURCE 3 ORGANISM_COMMON: YELLOW MEALWORM; SOURCE 4 ORGANISM_TAXID: 7067; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET20B; SOURCE 9 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN YELLOW MEAL WORM KEYWDS EF-HAND, ALL-ALPHA, ANTIFREEZE PROTEIN EXPDTA SOLUTION NMR NUMMDL 23 AUTHOR F.D.SOENNICHSEN REVDAT 4 16-FEB-22 1C3Y 1 REMARK REVDAT 3 24-FEB-09 1C3Y 1 VERSN REVDAT 2 01-APR-03 1C3Y 1 JRNL REVDAT 1 10-NOV-99 1C3Y 0 JRNL AUTH S.ROTHEMUND,Y.C.LIOU,P.L.DAVIES,E.KRAUSE,F.D.SONNICHSEN JRNL TITL A NEW CLASS OF HEXAHELICAL INSECT PROTEINS REVEALED AS JRNL TITL 2 PUTATIVE CARRIERS OF SMALL HYDROPHOBIC LIGANDS. JRNL REF STRUCTURE FOLD.DES. V. 7 1325 1999 JRNL REFN ISSN 0969-2126 JRNL PMID 10574794 JRNL DOI 10.1016/S0969-2126(00)80022-2 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH S ROTHEMUND,Y.-C.LIOU,P.L.DAVIES,F.D.SONNICHSEN REMARK 1 TITL BACKBONE STRUCTURE AND DYNAMICS OF A HEMOLYMPH PROTEIN FROM REMARK 1 TITL 2 THE MEALWORM BEETLE TENEBRIO MOLITOR REMARK 1 REF BIOCHEMISTRY V. 11 13791 1997 REMARK 1 REFN ISSN 0006-2960 REMARK 1 DOI 10.1021/BI971529K REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : NMRPIPE SGI6X.M4, X-PLOR 3.81 REMARK 3 AUTHORS : DELAGLIO, F. ET AL. (NMRPIPE), BRUENGER (X-PLOR) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1C3Y COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY NDB. REMARK 100 THE DEPOSITION ID IS D_1000001274. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 25; 25 REMARK 210 PH : 6.9; 6.9 REMARK 210 IONIC STRENGTH : NO SALT; NO SALT REMARK 210 PRESSURE : AMBIENT; AMBIENT REMARK 210 SAMPLE CONTENTS : 1MM PROTEIN, N15- OR N15/C13 REMARK 210 -DOUBLE LABELED; 1MM PROTEIN, REMARK 210 N15- OR N15/C13-DOUBLE LABELED REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C REMARK 210 -SEPARATED_NOESY; 4D_13C- REMARK 210 SEPARATED_NOESY; CBCACONNH; REMARK 210 HNCACB; HNHA REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ REMARK 210 SPECTROMETER MODEL : INOVA REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : PIPP 3.6.8, X-PLOR 3.81 REMARK 210 METHOD USED : ENSEMBLE OF 23 STRUCTURES REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL REMARK 210 CONFORMERS, NUMBER SUBMITTED : 23 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 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: 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 LEU A 7 -79.04 63.50 REMARK 500 1 LYS A 8 -165.42 -62.04 REMARK 500 1 GLN A 9 173.19 65.07 REMARK 500 1 GLU A 32 -76.58 -135.05 REMARK 500 1 GLU A 33 141.21 178.15 REMARK 500 1 ASP A 35 65.05 -150.56 REMARK 500 1 PHE A 52 -65.19 -100.89 REMARK 500 1 ASN A 71 83.82 60.48 REMARK 500 1 SER A 72 -42.10 -161.64 REMARK 500 1 HIS A 74 51.51 -150.65 REMARK 500 1 GLU A 76 -38.38 178.85 REMARK 500 1 ALA A 86 47.22 -84.65 REMARK 500 1 PHE A 100 32.19 -99.72 REMARK 500 1 LYS A 101 -55.64 -143.66 REMARK 500 1 HIS A 104 -52.62 -155.95 REMARK 500 1 ASP A 105 46.69 -99.86 REMARK 500 2 ARG A 4 149.42 62.73 REMARK 500 2 GLU A 5 -66.62 70.06 REMARK 500 2 LYS A 6 143.15 63.44 REMARK 500 2 ASP A 12 74.67 -64.05 REMARK 500 2 ALA A 13 -40.45 166.83 REMARK 500 2 SER A 18 -82.35 -74.74 REMARK 500 2 GLU A 23 -67.30 -123.01 REMARK 500 2 GLU A 32 -79.04 -147.60 REMARK 500 2 GLU A 33 -178.08 178.02 REMARK 500 2 VAL A 34 -66.61 -150.53 REMARK 500 2 ASP A 35 87.22 60.29 REMARK 500 2 ILE A 53 148.33 -179.13 REMARK 500 2 PHE A 59 93.69 39.42 REMARK 500 2 GLU A 76 -52.67 -156.29 REMARK 500 2 LYS A 77 54.14 -167.56 REMARK 500 2 ALA A 86 46.11 -84.70 REMARK 500 2 LYS A 101 -60.76 178.31 REMARK 500 3 GLU A 17 -50.71 -157.10 REMARK 500 3 GLU A 22 52.20 -91.80 REMARK 500 3 GLU A 33 138.52 63.98 REMARK 500 3 VAL A 34 125.96 -177.22 REMARK 500 3 ASP A 35 -64.50 -91.65 REMARK 500 3 ASP A 36 153.65 61.03 REMARK 500 3 ASN A 71 59.26 -179.40 REMARK 500 3 ALA A 86 33.98 -87.12 REMARK 500 3 PHE A 100 -39.12 177.64 REMARK 500 3 ASN A 106 70.57 60.33 REMARK 500 3 ARG A 107 -69.97 68.02 REMARK 500 4 LEU A 7 -68.73 68.04 REMARK 500 4 LYS A 8 94.53 60.28 REMARK 500 4 HIS A 10 179.40 59.84 REMARK 500 4 ASP A 12 79.69 -63.56 REMARK 500 4 ALA A 13 -36.66 169.29 REMARK 500 4 SER A 21 -170.55 55.36 REMARK 500 REMARK 500 THIS ENTRY HAS 356 RAMACHANDRAN 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 ARG A 4 0.28 SIDE CHAIN REMARK 500 1 ARG A 29 0.31 SIDE CHAIN REMARK 500 1 ARG A 31 0.19 SIDE CHAIN REMARK 500 1 ARG A 49 0.23 SIDE CHAIN REMARK 500 1 ARG A 107 0.27 SIDE CHAIN REMARK 500 2 ARG A 4 0.29 SIDE CHAIN REMARK 500 2 ARG A 29 0.30 SIDE CHAIN REMARK 500 2 ARG A 31 0.28 SIDE CHAIN REMARK 500 2 ARG A 49 0.21 SIDE CHAIN REMARK 500 2 ARG A 107 0.30 SIDE CHAIN REMARK 500 3 ARG A 4 0.19 SIDE CHAIN REMARK 500 3 ARG A 29 0.28 SIDE CHAIN REMARK 500 3 ARG A 31 0.23 SIDE CHAIN REMARK 500 3 ARG A 49 0.23 SIDE CHAIN REMARK 500 3 ARG A 107 0.30 SIDE CHAIN REMARK 500 4 ARG A 4 0.19 SIDE CHAIN REMARK 500 4 ARG A 29 0.29 SIDE CHAIN REMARK 500 4 ARG A 31 0.21 SIDE CHAIN REMARK 500 4 ARG A 49 0.31 SIDE CHAIN REMARK 500 4 ARG A 107 0.24 SIDE CHAIN REMARK 500 5 ARG A 4 0.25 SIDE CHAIN REMARK 500 5 ARG A 29 0.29 SIDE CHAIN REMARK 500 5 ARG A 31 0.31 SIDE CHAIN REMARK 500 5 ARG A 49 0.29 SIDE CHAIN REMARK 500 5 ARG A 107 0.26 SIDE CHAIN REMARK 500 6 ARG A 4 0.22 SIDE CHAIN REMARK 500 6 ARG A 29 0.30 SIDE CHAIN REMARK 500 6 ARG A 31 0.22 SIDE CHAIN REMARK 500 6 ARG A 49 0.18 SIDE CHAIN REMARK 500 6 ARG A 107 0.24 SIDE CHAIN REMARK 500 7 ARG A 4 0.22 SIDE CHAIN REMARK 500 7 ARG A 29 0.20 SIDE CHAIN REMARK 500 7 ARG A 31 0.30 SIDE CHAIN REMARK 500 7 ARG A 49 0.30 SIDE CHAIN REMARK 500 7 ARG A 107 0.27 SIDE CHAIN REMARK 500 8 ARG A 4 0.31 SIDE CHAIN REMARK 500 8 ARG A 29 0.29 SIDE CHAIN REMARK 500 8 ARG A 31 0.31 SIDE CHAIN REMARK 500 8 ARG A 49 0.21 SIDE CHAIN REMARK 500 8 ARG A 107 0.24 SIDE CHAIN REMARK 500 9 ARG A 4 0.28 SIDE CHAIN REMARK 500 9 ARG A 29 0.28 SIDE CHAIN REMARK 500 9 ARG A 31 0.20 SIDE CHAIN REMARK 500 9 ARG A 49 0.27 SIDE CHAIN REMARK 500 9 ARG A 107 0.21 SIDE CHAIN REMARK 500 10 ARG A 4 0.31 SIDE CHAIN REMARK 500 10 ARG A 29 0.21 SIDE CHAIN REMARK 500 10 ARG A 31 0.21 SIDE CHAIN REMARK 500 10 ARG A 49 0.29 SIDE CHAIN REMARK 500 10 ARG A 107 0.22 SIDE CHAIN REMARK 500 REMARK 500 THIS ENTRY HAS 115 PLANE DEVIATIONS. REMARK 500 REMARK 500 REMARK: NULL DBREF 1C3Y A 1 108 UNP Q27011 Q27011_TENMO 19 126 SEQRES 1 A 108 GLU THR PRO ARG GLU LYS LEU LYS GLN HIS SER ASP ALA SEQRES 2 A 108 CYS LYS ALA GLU SER GLY VAL SER GLU GLU SER LEU ASN SEQRES 3 A 108 LYS VAL ARG ASN ARG GLU GLU VAL ASP ASP PRO LYS LEU SEQRES 4 A 108 LYS GLU HIS ALA PHE CYS ILE LEU LYS ARG ALA GLY PHE SEQRES 5 A 108 ILE ASP ALA SER GLY GLU PHE GLN LEU ASP HIS ILE LYS SEQRES 6 A 108 THR LYS PHE LYS GLU ASN SER GLU HIS PRO GLU LYS VAL SEQRES 7 A 108 ASP ASP LEU VAL ALA LYS CYS ALA VAL LYS LYS ASP THR SEQRES 8 A 108 PRO GLN HIS SER SER ALA ASP PHE PHE LYS CYS VAL HIS SEQRES 9 A 108 ASP ASN ARG SER HELIX 1 1 ALA A 13 SER A 18 1 6 HELIX 2 2 GLU A 23 ARG A 29 1 7 HELIX 3 3 ASP A 36 GLY A 51 1 16 HELIX 4 4 GLN A 60 GLU A 70 1 11 HELIX 5 5 LYS A 77 ALA A 86 1 10 HELIX 6 6 THR A 91 VAL A 103 1 13 SSBOND 1 CYS A 14 CYS A 45 1555 1555 2.02 SSBOND 2 CYS A 85 CYS A 102 1555 1555 2.02 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 16 2 Bytes