Header list of 1f71.pdb file
Complete list - 16 20 Bytes
HEADER TRANSPORT PROTEIN 24-JUN-00 1F71 TITLE REFINED SOLUTION STRUCTURE OF CALMODULIN C-TERMINAL DOMAIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: CALMODULIN; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: C-TERMINAL DOMAIN; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: XENOPUS LAEVIS; SOURCE 3 ORGANISM_COMMON: AFRICAN CLAWED FROG; SOURCE 4 ORGANISM_TAXID: 8355; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 EXPRESSION_SYSTEM_VECTOR: PTNCO12 KEYWDS CALCIUM BINDING, EF HAND, FOUR-HELIX BUNDLE, TRANSPORT PROTEIN EXPDTA SOLUTION NMR NUMMDL 10 AUTHOR J.CHOU,S.LI,A.BAX REVDAT 5 16-FEB-22 1F71 1 REMARK REVDAT 4 24-FEB-09 1F71 1 VERSN REVDAT 3 01-APR-03 1F71 1 JRNL REVDAT 2 04-APR-01 1F71 1 JRNL REVDAT 1 22-SEP-00 1F71 0 JRNL AUTH J.J.CHOU,S.LI,A.BAX JRNL TITL STUDY OF CONFORMATIONAL REARRANGEMENT AND REFINEMENT OF JRNL TITL 2 STRUCTURAL HOMOLOGY MODELS BY THE USE OF HETERONUCLEAR JRNL TITL 3 DIPOLAR COUPLINGS. JRNL REF J.BIOMOL.NMR V. 18 217 2000 JRNL REFN ISSN 0925-2738 JRNL PMID 11142512 JRNL DOI 10.1023/A:1026563923774 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 2.6, X-PLOR 3.84 REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER (X-PLOR) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1F71 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-JUN-00. REMARK 100 THE DEPOSITION ID IS D_1000011322. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 7.0 REMARK 210 IONIC STRENGTH : 100MM KCL REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1 MM CALMODULIN U-15N,13C; 5 MM REMARK 210 HEPES BUFFER, 100 MM KCL; 1 MM REMARK 210 CALMODULIN U-15N,13C; 5 MM HEPES REMARK 210 BUFFER, 100 MM KCL; 21 MG/ML REMARK 210 FILAMENTOUS PHAGE PF1 REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D IPAP-HSQC (NO H1 DECOUPLING); REMARK 210 3D CT-(H)CA(CO)NH (NO H1 REMARK 210 DECOUPLING); 3D HNCO (NO CA REMARK 210 DECOUPLING) REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 600 MHZ; 500 MHZ REMARK 210 SPECTROMETER MODEL : DRX; DMX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRPIPE 1.8, NMRDRAW 1.8 REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 20 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST REMARK 210 ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 6 REMARK 210 REMARK 210 REMARK: THIS STRUCTURE WAS REFINED USING PREVIOUS NMR RESTRAINTS REMARK 210 AND NEWLY MEASURED DIPOLAR COUPLINGS 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 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (RES=RESIDUE NAME; REMARK 470 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 470 MODELS 1-10 REMARK 470 RES CSSEQI ATOMS REMARK 470 LYS A 148 O 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 ASN A 97 -76.24 -121.65 REMARK 500 1 LEU A 112 0.24 -64.05 REMARK 500 1 LYS A 115 58.00 -102.39 REMARK 500 1 ILE A 130 -77.84 -136.76 REMARK 500 1 ASP A 133 -32.03 -140.82 REMARK 500 2 ASN A 97 -76.56 -121.62 REMARK 500 2 LYS A 115 56.52 -103.20 REMARK 500 2 ILE A 130 -77.49 -137.19 REMARK 500 2 ASP A 133 -32.94 -140.86 REMARK 500 3 ASN A 97 -76.38 -121.58 REMARK 500 3 LYS A 115 56.76 -101.83 REMARK 500 3 ILE A 130 -77.94 -137.02 REMARK 500 3 ASP A 133 -32.75 -140.87 REMARK 500 4 ASN A 97 -75.80 -121.94 REMARK 500 4 LYS A 115 56.10 -101.60 REMARK 500 4 ILE A 130 -77.63 -137.04 REMARK 500 4 ASP A 133 -32.04 -140.88 REMARK 500 5 ASN A 97 -76.71 -123.17 REMARK 500 5 LYS A 115 58.21 -102.28 REMARK 500 5 ILE A 130 -77.61 -136.48 REMARK 500 5 ASP A 133 -33.02 -140.87 REMARK 500 6 ASN A 97 -75.95 -123.20 REMARK 500 6 LYS A 115 58.34 -102.23 REMARK 500 6 ILE A 130 -77.89 -137.24 REMARK 500 6 ASP A 133 -33.29 -140.85 REMARK 500 7 ASN A 97 -76.20 -121.49 REMARK 500 7 LYS A 115 55.96 -101.92 REMARK 500 7 ILE A 130 -77.83 -136.74 REMARK 500 7 ASP A 133 -31.35 -140.97 REMARK 500 8 ASN A 97 -76.72 -122.93 REMARK 500 8 LYS A 115 55.63 -101.57 REMARK 500 8 ILE A 130 -77.49 -136.69 REMARK 500 8 ASP A 133 -32.47 -140.69 REMARK 500 9 ASN A 97 -75.95 -123.20 REMARK 500 9 LYS A 115 58.34 -102.23 REMARK 500 9 ILE A 130 -77.89 -137.24 REMARK 500 9 ASP A 133 -33.29 -140.85 REMARK 500 10 ASN A 97 -76.56 -121.62 REMARK 500 10 LYS A 115 56.52 -103.20 REMARK 500 10 ILE A 130 -77.49 -137.19 REMARK 500 10 ASP A 133 -32.94 -140.86 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1F70 RELATED DB: PDB REMARK 900 N-TERMINAL DOMAIN OF CALMODULIN REFINED WITH DIPOLAR COUPLINGS REMARK 900 RELATED ID: 1CFC RELATED DB: PDB REMARK 900 SOLUTION STRUCTURE OF CALMODULIN REFINED WITHOUT DIPOLAR COUPLINGS REMARK 900 RELATED ID: 1DMO RELATED DB: PDB REMARK 900 SOLUTION STRUCTURE OF CALMODULIN REFINED WITHOUT DIPOLAR COUPLINGS DBREF 1F71 A 82 148 UNP P62155 CALM_XENLA 83 149 SEQRES 1 A 67 GLU GLU GLU ILE ARG GLU ALA PHE ARG VAL PHE ASP LYS SEQRES 2 A 67 ASP GLY ASN GLY TYR ILE SER ALA ALA GLU LEU ARG HIS SEQRES 3 A 67 VAL MET THR ASN LEU GLY GLU LYS LEU THR ASP GLU GLU SEQRES 4 A 67 VAL ASP GLU MET ILE ARG GLU ALA ASP ILE ASP GLY ASP SEQRES 5 A 67 GLY GLN VAL ASN TYR GLU GLU PHE VAL GLN MET MET THR SEQRES 6 A 67 ALA LYS HELIX 1 1 GLU A 82 PHE A 92 1 11 HELIX 2 2 ALA A 102 LEU A 112 1 11 HELIX 3 3 THR A 117 ALA A 128 1 12 HELIX 4 4 TYR A 138 LYS A 148 1 11 SHEET 1 A 2 TYR A 99 SER A 101 0 SHEET 2 A 2 GLN A 135 ASN A 137 -1 N VAL A 136 O ILE A 100 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 - 16 20 Bytes