Header list of 2al3.pdb file
Complete list - r 9 2 Bytes
HEADER ENDOCYTOSIS/EXOCYTOSIS 04-AUG-05 2AL3 TITLE SOLUTION STRUCTURE AND BACKBONE DYNAMICS OF AN N-TERMINAL UBIQUITIN- TITLE 2 LIKE DOMAIN IN THE GLUT4-TETHERING PROTEIN, TUG COMPND MOL_ID: 1; COMPND 2 MOLECULE: TUG LONG ISOFORM; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: N-TERMINAL UBIQUITIN-LIKE DOMAIN (RESIDUES 1-90); COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE; SOURCE 4 ORGANISM_TAXID: 10090; SOURCE 5 GENE: TUG; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 DE3; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX-2K KEYWDS TUG UBL1 INSULIN, ENDOCYTOSIS-EXOCYTOSIS COMPLEX EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR M.C.TETTAMANZI,C.YU,J.S.BOGAN,M.E.HODSDON REVDAT 3 09-MAR-22 2AL3 1 REMARK REVDAT 2 24-FEB-09 2AL3 1 VERSN REVDAT 1 21-MAR-06 2AL3 0 JRNL AUTH M.C.TETTAMANZI,C.YU,J.S.BOGAN,M.E.HODSDON JRNL TITL SOLUTION STRUCTURE AND BACKBONE DYNAMICS OF AN N-TERMINAL JRNL TITL 2 UBIQUITIN-LIKE DOMAIN IN THE GLUT4-REGULATING PROTEIN, TUG. JRNL REF PROTEIN SCI. V. 15 498 2006 JRNL REFN ISSN 0961-8368 JRNL PMID 16501224 JRNL DOI 10.1110/PS.051901806 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CYANA 1.0.5 REMARK 3 AUTHORS : P.GUNTERT ET AL. REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 2AL3 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-AUG-05. REMARK 100 THE DEPOSITION ID IS D_1000034021. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 7.4 REMARK 210 IONIC STRENGTH : 20 MM NACL REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 0.75 MM TUG-UBL1, 20 MM REMARK 210 POTASSIUM PHOSPHATE, 20 MM NACL, REMARK 210 0.05% NAN3, 1 UM LUPEPTIN, 1 UM REMARK 210 PEPSTATIN, 1 UM PMSF, 1.5 MM REMARK 210 PROTEIN, UNIFORM (RANDOM) REMARK 210 LABELING WITH 13C, 15N AT KNOWN REMARK 210 LABELING REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 4D_13C/15N-SEPARATED_NOESY; REMARK 210 3D_13C-SEPARATED_NOESY; 3D_15N - REMARK 210 SEPARATED_NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : INOVA REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : VNMR 6.1, NMRDRAW 2.1, NMRPIPE, REMARK 210 SPARKY 3.98, NMRVIEW 5.0.4, REMARK 210 CYANA 1.0.5, TALOS REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 20 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST REMARK 210 RESTRAINT VIOLATIONS REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 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 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 1-20 REMARK 465 RES C SSSEQI REMARK 465 MET A 1 REMARK 465 ALA A 2 REMARK 465 ALA A 3 REMARK 465 PRO A 4 REMARK 465 ALA A 5 REMARK 465 GLY A 6 REMARK 465 GLY A 7 REMARK 465 GLY A 8 REMARK 465 GLY A 9 REMARK 465 GLU A 86 REMARK 465 GLY A 87 REMARK 465 PRO A 88 REMARK 465 GLU A 89 REMARK 465 ASN A 90 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 H ASP A 51 O VAL A 79 1.26 REMARK 500 O LEU A 52 H LEU A 59 1.32 REMARK 500 O SER A 13 H LEU A 76 1.36 REMARK 500 O LEU A 32 H LEU A 36 1.46 REMARK 500 O GLN A 64 H ALA A 68 1.49 REMARK 500 HG1 THR A 39 OE1 GLN A 43 1.51 REMARK 500 H SER A 13 O ALA A 74 1.52 REMARK 500 H PHE A 54 O THR A 57 1.53 REMARK 500 O PHE A 67 HD21 ASN A 69 1.58 REMARK 500 O LEU A 52 N LEU A 59 2.19 REMARK 500 O VAL A 12 O VAL A 24 2.19 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 ASP A 44 69.54 33.75 REMARK 500 1 GLN A 55 -109.08 60.65 REMARK 500 1 ASP A 60 -147.46 -145.76 REMARK 500 1 SER A 62 41.44 -88.19 REMARK 500 1 ASN A 69 94.00 42.82 REMARK 500 1 ASN A 72 -85.30 -40.59 REMARK 500 1 ALA A 74 83.78 27.01 REMARK 500 1 VAL A 81 -166.19 165.15 REMARK 500 1 ARG A 83 173.08 51.46 REMARK 500 2 ASP A 44 67.16 39.83 REMARK 500 2 GLN A 55 -104.02 56.56 REMARK 500 2 ASP A 60 -153.61 -138.18 REMARK 500 2 SER A 62 40.06 -85.91 REMARK 500 2 ASN A 69 93.71 40.79 REMARK 500 2 ASN A 72 -90.10 -35.84 REMARK 500 2 ALA A 74 88.83 24.35 REMARK 500 2 VAL A 81 -154.79 162.04 REMARK 500 3 GLN A 55 -107.30 59.63 REMARK 500 3 ASP A 60 -149.45 -142.07 REMARK 500 3 SER A 62 38.27 -85.63 REMARK 500 3 ASN A 69 95.42 42.50 REMARK 500 3 ASN A 72 -87.95 -37.76 REMARK 500 3 ALA A 74 90.83 22.33 REMARK 500 3 VAL A 81 -154.46 160.79 REMARK 500 3 ARG A 83 129.18 -39.37 REMARK 500 3 SER A 84 159.59 61.97 REMARK 500 4 GLN A 55 -108.04 58.95 REMARK 500 4 ASP A 60 -148.82 -144.36 REMARK 500 4 SER A 62 39.88 -88.70 REMARK 500 4 ASN A 69 90.98 40.70 REMARK 500 4 ASN A 72 -76.01 -45.34 REMARK 500 4 ALA A 74 84.60 24.05 REMARK 500 4 VAL A 81 -153.68 159.87 REMARK 500 4 SER A 84 82.10 65.48 REMARK 500 5 GLN A 55 -105.81 56.78 REMARK 500 5 ASP A 60 -154.14 -139.17 REMARK 500 5 SER A 62 39.57 -85.02 REMARK 500 5 ASN A 69 92.70 42.05 REMARK 500 5 ASN A 72 -82.45 -43.42 REMARK 500 5 ALA A 74 89.09 23.23 REMARK 500 5 VAL A 81 -150.92 160.30 REMARK 500 6 GLN A 55 -106.72 60.09 REMARK 500 6 ASP A 60 -152.64 -139.66 REMARK 500 6 SER A 62 40.74 -85.90 REMARK 500 6 PHE A 67 -62.98 -103.67 REMARK 500 6 ASN A 69 93.32 41.48 REMARK 500 6 ASN A 72 -82.93 -40.71 REMARK 500 6 ALA A 74 88.16 27.19 REMARK 500 6 VAL A 81 -149.82 161.17 REMARK 500 7 ASP A 44 66.81 34.87 REMARK 500 REMARK 500 THIS ENTRY HAS 169 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 999 REMARK 999 SEQUENCE REMARK 999 THE MISSING RESIDUES ARE THE RESULTS OF STRUCTURAL REMARK 999 DISORDER AND DEGRADATION DURING THE EXPERIMENTS. DBREF 2AL3 A 1 90 GB 37704773 AAR01614 1 90 SEQRES 1 A 90 MET ALA ALA PRO ALA GLY GLY GLY GLY SER ALA VAL SER SEQRES 2 A 90 VAL LEU ALA PRO ASN GLY ARG ARG HIS THR VAL LYS VAL SEQRES 3 A 90 THR PRO SER THR VAL LEU LEU GLN VAL LEU GLU ASP THR SEQRES 4 A 90 CYS ARG ARG GLN ASP PHE ASN PRO SER GLU TYR ASP LEU SEQRES 5 A 90 LYS PHE GLN ARG THR VAL LEU ASP LEU SER LEU GLN TRP SEQRES 6 A 90 ARG PHE ALA ASN LEU PRO ASN ASN ALA LYS LEU GLU MET SEQRES 7 A 90 VAL PRO VAL SER ARG SER ARG GLU GLY PRO GLU ASN HELIX 1 1 VAL A 31 GLN A 43 1 13 HELIX 2 2 ASN A 46 TYR A 50 5 5 HELIX 3 3 GLN A 64 ASN A 69 1 6 SHEET 1 A 5 ARG A 21 VAL A 24 0 SHEET 2 A 5 VAL A 12 LEU A 15 -1 N VAL A 14 O HIS A 22 SHEET 3 A 5 LYS A 75 VAL A 79 1 O LEU A 76 N SER A 13 SHEET 4 A 5 ASP A 51 PHE A 54 -1 N ASP A 51 O VAL A 79 SHEET 5 A 5 THR A 57 LEU A 59 -1 O LEU A 59 N LEU A 52 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