Header list of 1aey.pdb file
Complete list - b 16 2 Bytes
HEADER CYTOSKELETON 02-MAR-97 1AEY TITLE ALPHA-SPECTRIN SRC HOMOLOGY 3 DOMAIN, SOLUTION NMR, 15 STRUCTURES COMPND MOL_ID: 1; COMPND 2 MOLECULE: ALPHA-SPECTRIN; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: SRC HOMOLOGY 3 DOMAIN; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: GALLUS GALLUS; SOURCE 3 ORGANISM_COMMON: CHICKEN; SOURCE 4 ORGANISM_TAXID: 9031; SOURCE 5 ORGAN: BRAIN; SOURCE 6 CELLULAR_LOCATION: CYTOSKELETON; SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET3D KEYWDS CYTOSKELETON, CAPPING PROTEIN, CALCIUM-BINDING, DUPLICATION, SH3 KEYWDS 2 DOMAIN EXPDTA SOLUTION NMR NUMMDL 15 AUTHOR F.J.BLANCO,A.R.ORTIZ,L.SERRANO REVDAT 3 16-FEB-22 1AEY 1 REMARK REVDAT 2 24-FEB-09 1AEY 1 VERSN REVDAT 1 15-MAY-97 1AEY 0 JRNL AUTH F.J.BLANCO,A.R.ORTIZ,L.SERRANO JRNL TITL 1H AND 15N NMR ASSIGNMENT AND SOLUTION STRUCTURE OF THE SH3 JRNL TITL 2 DOMAIN OF SPECTRIN: COMPARISON OF UNREFINED AND REFINED JRNL TITL 3 STRUCTURE SETS WITH THE CRYSTAL STRUCTURE. JRNL REF J.BIOMOL.NMR V. 9 347 1997 JRNL REFN ISSN 0925-2738 JRNL PMID 9255941 JRNL DOI 10.1023/A:1018330122908 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH A.R.VIGUERA,L.SERRANO,M.WILMANNS REMARK 1 TITL DIFFERENT FOLDING TRANSITION STATES MAY RESULT IN THE SAME REMARK 1 TITL 2 NATIVE STRUCTURE REMARK 1 REF NAT.STRUCT.BIOL. V. 3 874 1996 REMARK 1 REFN ISSN 1072-8368 REMARK 1 REFERENCE 2 REMARK 1 AUTH A.MUSACCHIO,M.NOBLE,R.PAUPTIT,R.WIERENGA,M.SARASTE REMARK 1 TITL CRYSTAL STRUCTURE OF A SRC-HOMOLOGY 3 (SH3) DOMAIN REMARK 1 REF NATURE V. 359 851 1992 REMARK 1 REFN ISSN 0028-0836 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : AMBER REMARK 3 AUTHORS : PEARLMAN,CASE,CALDWELL,ROSS,CHEATHAM, REMARK 3 FERGUSON,SEIBEL,SINGH,WEINER,KOLLMAN REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE FINAL MODELS WERE ENERGY MINIMIZED REMARK 3 IN A SHELL OF WATER MOLECULES USING THE AMBER ALL ATOM FORCE REMARK 3 FIELD. REMARK 4 REMARK 4 1AEY 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_1000170733. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 297 REMARK 210 PH : 3.5 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; TOCSY; COSY; HMQC-TOCSY; REMARK 210 HMQC-NOESY; E.COSY REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ REMARK 210 SPECTROMETER MODEL : AMX500 REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : UXNMR, AURELIA, DIANA, AMBER REMARK 210 METHOD USED : VARIABLE TARGET FUNCTION REMARK 210 SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 15 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15 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 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 1-15 REMARK 465 RES C SSSEQI REMARK 465 MET A 1 REMARK 465 ASP A 2 REMARK 465 GLU A 3 REMARK 465 THR A 4 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 15 ASP A 48 CB - CA - C ANGL. DEV. = -12.8 DEGREES REMARK 500 15 ARG A 49 N - CA - CB ANGL. DEV. = -11.8 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 LYS A 6 -142.17 -76.87 REMARK 500 1 LYS A 39 -51.00 75.25 REMARK 500 1 ASN A 47 -72.85 60.12 REMARK 500 1 ASP A 48 11.59 -150.93 REMARK 500 2 LYS A 6 -125.94 -70.92 REMARK 500 2 LEU A 34 -66.53 -98.11 REMARK 500 2 ASP A 40 -53.13 -130.22 REMARK 500 2 ASN A 47 -80.81 65.11 REMARK 500 3 LYS A 6 -153.49 -109.75 REMARK 500 3 SER A 36 49.44 -84.30 REMARK 500 3 ASN A 47 -77.93 61.46 REMARK 500 4 GLU A 17 152.08 -47.14 REMARK 500 4 ASP A 40 -65.35 -107.74 REMARK 500 4 ASN A 47 -76.46 63.93 REMARK 500 5 SER A 36 53.12 -116.61 REMARK 500 5 ASN A 47 -86.56 65.70 REMARK 500 6 LYS A 6 95.34 58.68 REMARK 500 6 SER A 36 43.82 -109.41 REMARK 500 6 THR A 37 37.76 -88.73 REMARK 500 6 ASN A 47 -74.34 62.98 REMARK 500 6 ASP A 48 22.34 -160.18 REMARK 500 7 LYS A 6 -152.99 -104.67 REMARK 500 7 ASN A 47 -71.25 67.49 REMARK 500 8 LYS A 6 -140.14 -81.93 REMARK 500 8 ASP A 40 -61.13 -152.86 REMARK 500 8 ASN A 47 -69.08 67.07 REMARK 500 8 ASP A 48 15.27 -154.04 REMARK 500 9 THR A 37 1.69 -61.43 REMARK 500 9 LYS A 39 -59.89 72.61 REMARK 500 9 ASP A 40 -64.27 -90.43 REMARK 500 9 ASN A 47 -85.53 61.28 REMARK 500 10 LYS A 6 95.73 59.66 REMARK 500 10 GLU A 17 132.67 -39.63 REMARK 500 10 ASN A 47 -88.71 58.18 REMARK 500 10 LEU A 61 38.77 -93.37 REMARK 500 11 ASN A 47 -74.99 67.05 REMARK 500 12 ASN A 47 -63.16 71.36 REMARK 500 12 ASP A 48 -1.45 -153.35 REMARK 500 12 GLN A 50 76.92 -101.10 REMARK 500 13 LEU A 34 -32.60 -146.37 REMARK 500 13 ASP A 40 -52.05 -159.17 REMARK 500 13 ASN A 47 -77.11 58.52 REMARK 500 13 LEU A 61 42.25 -96.58 REMARK 500 14 LYS A 6 48.25 -158.07 REMARK 500 14 LEU A 34 -72.24 -79.89 REMARK 500 14 ASN A 47 -71.49 64.79 REMARK 500 14 ASP A 48 22.55 -156.38 REMARK 500 15 LYS A 6 58.96 -95.02 REMARK 500 15 LEU A 34 -48.89 -145.48 REMARK 500 15 SER A 36 25.92 -141.58 REMARK 500 REMARK 500 THIS ENTRY HAS 51 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 2 TYR A 13 0.06 SIDE CHAIN REMARK 500 2 TYR A 15 0.09 SIDE CHAIN REMARK 500 2 ARG A 21 0.10 SIDE CHAIN REMARK 500 3 ARG A 21 0.11 SIDE CHAIN REMARK 500 3 ARG A 49 0.08 SIDE CHAIN REMARK 500 4 TYR A 13 0.09 SIDE CHAIN REMARK 500 5 TYR A 15 0.07 SIDE CHAIN REMARK 500 5 ARG A 21 0.11 SIDE CHAIN REMARK 500 7 TYR A 13 0.07 SIDE CHAIN REMARK 500 7 TYR A 15 0.08 SIDE CHAIN REMARK 500 9 TYR A 13 0.07 SIDE CHAIN REMARK 500 10 TYR A 13 0.07 SIDE CHAIN REMARK 500 11 TYR A 13 0.07 SIDE CHAIN REMARK 500 12 TYR A 15 0.09 SIDE CHAIN REMARK 500 12 ARG A 21 0.09 SIDE CHAIN REMARK 500 12 ARG A 49 0.10 SIDE CHAIN REMARK 500 14 TYR A 15 0.11 SIDE CHAIN REMARK 500 15 TYR A 15 0.07 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL DBREF 1AEY A 2 62 UNP P07751 SPTA2_CHICK 965 1025 SEQRES 1 A 62 MET ASP GLU THR GLY LYS GLU LEU VAL LEU ALA LEU TYR SEQRES 2 A 62 ASP TYR GLN GLU LYS SER PRO ARG GLU VAL THR MET LYS SEQRES 3 A 62 LYS GLY ASP ILE LEU THR LEU LEU ASN SER THR ASN LYS SEQRES 4 A 62 ASP TRP TRP LYS VAL GLU VAL ASN ASP ARG GLN GLY PHE SEQRES 5 A 62 VAL PRO ALA ALA TYR VAL LYS LYS LEU ASP HELIX 1 1 ALA A 55 TYR A 57 5 3 SHEET 1 A 5 VAL A 58 ASP A 62 0 SHEET 2 A 5 GLU A 7 ALA A 11 -1 N LEU A 10 O LYS A 59 SHEET 3 A 5 ILE A 30 ASN A 35 -1 N LEU A 33 O GLU A 7 SHEET 4 A 5 TRP A 41 VAL A 46 -1 N GLU A 45 O THR A 32 SHEET 5 A 5 ARG A 49 PRO A 54 -1 N VAL A 53 O TRP A 42 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