Header list of 1ksr.pdb file
Complete list - b 23 2 Bytes
HEADER ACTIN BINDING PROTEIN 07-FEB-97 1KSR TITLE THE REPEATING SEGMENTS OF THE F-ACTIN CROSS-LINKING GELATION FACTOR TITLE 2 (ABP-120) HAVE AN IMMUNOGLOBULIN FOLD, NMR, 20 STRUCTURES COMPND MOL_ID: 1; COMPND 2 MOLECULE: GELATION FACTOR; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: ROD 4; COMPND 5 SYNONYM: ABP-120; COMPND 6 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: DICTYOSTELIUM DISCOIDEUM; SOURCE 3 ORGANISM_TAXID: 44689; SOURCE 4 STRAIN: AX3; SOURCE 5 CELL_LINE: BL21; SOURCE 6 CELLULAR_LOCATION: CYTOPLASM, CELL CORTEX; SOURCE 7 GENE: ABPC; SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 9 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 10 EXPRESSION_SYSTEM_STRAIN: BL21 (DE); SOURCE 11 EXPRESSION_SYSTEM_CELLULAR_LOCATION: CYTOPLASM; SOURCE 12 EXPRESSION_SYSTEM_VECTOR_TYPE: T7 PROMOTER; SOURCE 13 EXPRESSION_SYSTEM_PLASMID: PT7-7; SOURCE 14 EXPRESSION_SYSTEM_GENE: T7 KEYWDS ACTIN BINDING PROTEIN, IMMUNOGLOBULIN, GELATION FACTOR, ABP-120 EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR P.FUCINI,C.RENNER,C.HERBERHOLD,A.A.NOEGEL,T.A.HOLAK REVDAT 3 23-FEB-22 1KSR 1 REMARK REVDAT 2 24-FEB-09 1KSR 1 VERSN REVDAT 1 20-AUG-97 1KSR 0 JRNL AUTH P.FUCINI,C.RENNER,C.HERBERHOLD,A.A.NOEGEL,T.A.HOLAK JRNL TITL THE REPEATING SEGMENTS OF THE F-ACTIN CROSS-LINKING GELATION JRNL TITL 2 FACTOR (ABP-120) HAVE AN IMMUNOGLOBULIN-LIKE FOLD. JRNL REF NAT.STRUCT.BIOL. V. 4 223 1997 JRNL REFN ISSN 1072-8368 JRNL PMID 9164464 JRNL DOI 10.1038/NSB0397-223 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH J.B.GORLIN,R.YAMIN,S.EGAN,M.STEWART,T.P.STOSSEL, REMARK 1 AUTH 2 D.J.KWIATKOWSKI,J.H.HARTWIG REMARK 1 TITL HUMAN ENDOTHELIAL ACTIN-BINDING PROTEIN (ABP-280, NONMUSCLE REMARK 1 TITL 2 FILAMIN): A MOLECULAR LEAF SPRING REMARK 1 REF J.CELL BIOL. V. 111 1089 1990 REMARK 1 REFN ISSN 0021-9525 REMARK 1 REFERENCE 2 REMARK 1 AUTH A.A.NOEGEL,S.RAPP,F.LOTTSPEICH,M.SCHLEICHER,M.STEWART REMARK 1 TITL THE DICTYOSTELIUM GELATION FACTOR SHARES A PUTATIVE ACTIN REMARK 1 TITL 2 BINDING SITE WITH ALPHA-ACTININS AND DYSTROPHIN AND ALSO HAS REMARK 1 TITL 3 A ROD DOMAIN CONTAINING SIX 100-RESIDUE MOTIFS THAT APPEAR REMARK 1 TITL 4 TO HAVE A CROSS-BETA CONFORMATION REMARK 1 REF J.CELL BIOL. V. 109 607 1989 REMARK 1 REFN ISSN 0021-9525 REMARK 1 REFERENCE 3 REMARK 1 AUTH J.M.CARBONI,J.S.CONDEELIS REMARK 1 TITL LIGAND-INDUCED CHANGES IN THE LOCATION OF ACTIN, MYOSIN, 95K REMARK 1 TITL 2 (ALPHA-ACTININ), AND 120K PROTEIN IN AMEBAE OF DICTYOSTELIUM REMARK 1 TITL 3 DISCOIDEUM REMARK 1 REF J.CELL BIOL. V. 100 1884 1985 REMARK 1 REFN ISSN 0021-9525 REMARK 1 REFERENCE 4 REMARK 1 AUTH J.CONDEELIS,M.VAHEY,J.M.CARBONI,J.DEMEY,S.OGIHARA REMARK 1 TITL PROPERTIES OF THE 120,000-AND 95,000-DALTON ACTIN-BINDING REMARK 1 TITL 2 PROTEINS FROM DICTYOSTELIUM DISCOIDEUM AND THEIR POSSIBLE REMARK 1 TITL 3 FUNCTIONS IN ASSEMBLING THE CYTOPLASMIC MATRIX REMARK 1 REF J.CELL BIOL. V. 99 119S 1984 REMARK 1 REFN ISSN 0021-9525 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1KSR 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_1000174489. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 304 REMARK 210 PH : 7.0 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : HNCA; CBCA(CO)NH; HSQC; 2D REMARK 210 NOESY; 3D NOESY; 3D TOCSY; 2D REMARK 210 TOCSY. REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 750 MHZ REMARK 210 SPECTROMETER MODEL : DRX; AMX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : CCNMR (HOME MADE) MADE), X-PLOR, REMARK 210 UXNMR (BRUKER). UXNMR (BRUKER). REMARK 210 (BRUKER). REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED REMARK 210 ANNEALING, ENERGY MINIMIZATION. REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 45 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : NUMBER (0) OF RESIDUAL REMARK 210 CONSTRAINS VIOLATION (THRESHOLDS: REMARK 210 0.45 A FOR NOES AND 10.0 DEGREE REMARK 210 FOR ANGLES) 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 H ILE A 26 O TYR A 65 1.47 REMARK 500 H TYR A 77 O VAL A 95 1.49 REMARK 500 OD2 ASP A 2 H VAL A 29 1.51 REMARK 500 H THR A 46 O ASN A 80 1.52 REMARK 500 O ASP A 41 H PHE A 43 1.55 REMARK 500 H ASP A 30 O VAL A 34 1.59 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 5 35.91 -147.58 REMARK 500 1 LEU A 13 -8.71 90.12 REMARK 500 1 PRO A 31 21.58 -77.65 REMARK 500 1 HIS A 35 54.23 -98.20 REMARK 500 1 ARG A 36 70.32 65.02 REMARK 500 1 THR A 37 85.00 43.01 REMARK 500 1 ASP A 38 153.21 -42.73 REMARK 500 1 GLU A 73 -141.37 -152.30 REMARK 500 1 ASP A 84 -21.50 141.31 REMARK 500 1 PRO A 99 91.06 -69.09 REMARK 500 2 LYS A 5 38.16 -145.35 REMARK 500 2 LEU A 13 -6.30 90.32 REMARK 500 2 ASP A 30 -169.97 -113.45 REMARK 500 2 PRO A 31 32.34 -80.04 REMARK 500 2 ARG A 36 65.61 63.00 REMARK 500 2 THR A 37 90.22 46.32 REMARK 500 2 ASP A 38 149.70 -39.48 REMARK 500 2 ASP A 54 -66.78 -90.58 REMARK 500 2 LYS A 72 32.00 -141.67 REMARK 500 2 ASP A 84 -20.84 141.11 REMARK 500 2 LYS A 98 -63.84 -122.89 REMARK 500 3 LYS A 5 36.85 -142.75 REMARK 500 3 LEU A 13 -5.81 83.83 REMARK 500 3 HIS A 35 60.76 -104.89 REMARK 500 3 THR A 37 82.77 42.50 REMARK 500 3 ASP A 38 163.03 -41.44 REMARK 500 3 VAL A 53 77.11 -102.28 REMARK 500 3 ASP A 62 30.23 -91.69 REMARK 500 3 LYS A 72 32.67 -142.51 REMARK 500 3 GLU A 73 -151.13 -152.43 REMARK 500 3 ASP A 84 -23.07 141.56 REMARK 500 3 ASN A 89 22.29 -79.54 REMARK 500 3 PRO A 99 86.92 -69.04 REMARK 500 4 GLU A 4 10.04 -142.00 REMARK 500 4 LEU A 13 -8.30 86.60 REMARK 500 4 PRO A 31 20.64 -78.26 REMARK 500 4 HIS A 35 55.86 -101.10 REMARK 500 4 THR A 37 93.83 48.29 REMARK 500 4 ASP A 38 177.93 -45.75 REMARK 500 4 GLU A 73 -151.83 -152.50 REMARK 500 4 ASP A 84 -21.97 141.51 REMARK 500 4 PRO A 99 86.37 -68.67 REMARK 500 5 GLU A 4 13.87 -141.57 REMARK 500 5 LYS A 5 34.19 -141.23 REMARK 500 5 LEU A 13 -6.91 90.01 REMARK 500 5 ARG A 36 69.07 63.34 REMARK 500 5 THR A 37 87.67 44.01 REMARK 500 5 ASP A 38 148.51 -39.60 REMARK 500 5 PRO A 71 -157.82 -79.34 REMARK 500 5 LYS A 72 -59.34 -145.57 REMARK 500 REMARK 500 THIS ENTRY HAS 201 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 36 0.30 SIDE CHAIN REMARK 500 2 ARG A 36 0.22 SIDE CHAIN REMARK 500 3 ARG A 36 0.14 SIDE CHAIN REMARK 500 4 ARG A 36 0.14 SIDE CHAIN REMARK 500 5 ARG A 36 0.25 SIDE CHAIN REMARK 500 6 ARG A 36 0.22 SIDE CHAIN REMARK 500 7 ARG A 36 0.19 SIDE CHAIN REMARK 500 9 ARG A 36 0.27 SIDE CHAIN REMARK 500 11 ARG A 36 0.29 SIDE CHAIN REMARK 500 12 ARG A 36 0.31 SIDE CHAIN REMARK 500 13 ARG A 36 0.16 SIDE CHAIN REMARK 500 14 ARG A 36 0.29 SIDE CHAIN REMARK 500 15 ARG A 36 0.31 SIDE CHAIN REMARK 500 16 ARG A 36 0.28 SIDE CHAIN REMARK 500 17 ARG A 36 0.30 SIDE CHAIN REMARK 500 18 ARG A 36 0.23 SIDE CHAIN REMARK 500 19 ARG A 36 0.24 SIDE CHAIN REMARK 500 20 ARG A 36 0.27 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL DBREF 1KSR A 1 100 UNP P13466 GELA_DICDI 549 648 SEQRES 1 A 100 ALA ASP PRO GLU LYS SER TYR ALA GLU GLY PRO GLY LEU SEQRES 2 A 100 ASP GLY GLY GLU CYS PHE GLN PRO SER LYS PHE LYS ILE SEQRES 3 A 100 HIS ALA VAL ASP PRO ASP GLY VAL HIS ARG THR ASP GLY SEQRES 4 A 100 GLY ASP GLY PHE VAL VAL THR ILE GLU GLY PRO ALA PRO SEQRES 5 A 100 VAL ASP PRO VAL MET VAL ASP ASN GLY ASP GLY THR TYR SEQRES 6 A 100 ASP VAL GLU PHE GLU PRO LYS GLU ALA GLY ASP TYR VAL SEQRES 7 A 100 ILE ASN LEU THR LEU ASP GLY ASP ASN VAL ASN GLY PHE SEQRES 8 A 100 PRO LYS THR VAL THR VAL LYS PRO ALA SHEET 1 A 4 SER A 6 GLU A 9 0 SHEET 2 A 4 SER A 22 ALA A 28 -1 N HIS A 27 O TYR A 7 SHEET 3 A 4 THR A 64 PHE A 69 -1 N PHE A 69 O SER A 22 SHEET 4 A 4 MET A 57 ASP A 59 -1 N VAL A 58 O ASP A 66 SHEET 1 B 3 PHE A 43 GLU A 48 0 SHEET 2 B 3 GLY A 75 LEU A 83 -1 N THR A 82 O VAL A 44 SHEET 3 B 3 THR A 94 VAL A 97 -1 N VAL A 97 O GLY A 75 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 23 2 Bytes