Header list of 1z7t.pdb file
Complete list - r 2 2 Bytes
HEADER TRANSPORT PROTEIN 28-MAR-05 1Z7T TITLE SOLUTION STRUCTURE OF BACILLUS SUBTILIS BLAP APO-FORM COMPND MOL_ID: 1; COMPND 2 MOLECULE: BIOTIN/LIPOYL ATTACHMENT PROTEIN; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS SUBSP. SUBTILIS STR. 168; SOURCE 3 ORGANISM_TAXID: 224308; SOURCE 4 STRAIN: SUBSP. SUBTILIS STR. 168; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET 21A(+) KEYWDS BACILLUS SUBTILIS, SINGLE-DOMAIN BIOTIN CARBOXYL CARRIER PROTEIN, KEYWDS 2 SOLUTION STRUCTURE, APO-FORM, STRUCTURAL GENOMICS, TRANSPORT PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR G.CUI,B.XIA REVDAT 3 02-MAR-22 1Z7T 1 REMARK REVDAT 2 24-FEB-09 1Z7T 1 VERSN REVDAT 1 06-JUN-06 1Z7T 0 JRNL AUTH G.CUI,B.XIA JRNL TITL SOLUTION STRUCTURE OF BACILLUS SUBTILIS BLAP APO-FORM JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 3.5, AMBER 7.0 REMARK 3 AUTHORS : BRUKER (XWINNMR), REMARK 3 PEARLMAN,CASE,CALDWELL,ROSS,CHEATHAM,FERGUSON,SEIBEL,SINGH, REMARK 3 WEINER,KOLLMAN (AMBER) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 4125 RESTRAINTS. 3731 ARE REMARK 3 NOE-DERIVED REMARK 3 DISTANCE CONSTRAINTS, 109 DIHEDRAL ANGLE RESTRAINTS,28 DISTANCE REMARK 3 RESTRAINTS FROM HYDROGEN BONDS, 257 CHARITY RESTRAINTS. REMARK 4 REMARK 4 1Z7T COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 04-APR-05. REMARK 100 THE DEPOSITION ID IS D_1000032406. 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 : 150MM REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1.2MM S-BCCP U-15N, 13C; 50MM REMARK 210 PHOSPHATE BUFFER NA; 90% H2O, 10% REMARK 210 D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N REMARK 210 -SEPARATED_NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : AVANCE REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRPIPE 2.1, NMRVIEW 5, CYANA REMARK 210 1.0.6 REMARK 210 METHOD USED : SIMULATED ANNEALING MOLECULAR REMARK 210 DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 200 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST REMARK 210 ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 3D REMARK 210 HETERONUCLEAR TECHNIQUES. 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 TRP A 12 -60.11 -27.18 REMARK 500 1 VAL A 28 -37.36 -134.44 REMARK 500 2 TRP A 12 -59.79 -26.47 REMARK 500 3 TRP A 12 -59.21 -28.48 REMARK 500 4 THR A 72 26.60 -76.27 REMARK 500 5 VAL A 28 -37.94 -134.44 REMARK 500 5 MET A 34 44.98 39.77 REMARK 500 5 VAL A 48 98.99 -68.54 REMARK 500 5 THR A 72 -41.24 -130.54 REMARK 500 6 VAL A 28 -30.69 -134.63 REMARK 500 7 SER A 69 44.58 -79.01 REMARK 500 8 VAL A 28 -38.35 -134.93 REMARK 500 9 TRP A 12 -60.27 -27.49 REMARK 500 9 VAL A 28 -38.70 -135.14 REMARK 500 10 VAL A 28 -35.52 -141.26 REMARK 500 10 ASN A 70 28.62 -79.22 REMARK 500 10 SER A 71 49.99 -78.82 REMARK 500 11 LEU A 65 -51.61 -120.17 REMARK 500 11 ASN A 70 -51.82 -161.16 REMARK 500 12 TRP A 12 -59.87 -24.82 REMARK 500 12 SER A 69 30.75 -75.57 REMARK 500 14 TRP A 12 -59.82 -25.76 REMARK 500 15 TRP A 12 -59.26 -29.57 REMARK 500 15 VAL A 28 -31.15 -138.73 REMARK 500 19 SER A 71 72.56 -69.87 REMARK 500 20 TRP A 12 -59.10 -27.68 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 15 ARG A 44 0.11 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL DBREF 1Z7T A 2 73 UNP Q9R9I3 Q9R9I3_BACSU 2 73 SEQRES 1 A 72 THR VAL SER ILE GLN MET ALA GLY ASN LEU TRP LYS VAL SEQRES 2 A 72 HIS VAL LYS ALA GLY ASP GLN ILE GLU LYS GLY GLN GLU SEQRES 3 A 72 VAL ALA ILE LEU GLU SER MET LYS MET GLU ILE PRO ILE SEQRES 4 A 72 VAL ALA ASP ARG SER GLY ILE VAL LYS GLU VAL LYS LYS SEQRES 5 A 72 LYS GLU GLY ASP PHE VAL ASN GLU GLY ASP VAL LEU LEU SEQRES 6 A 72 GLU LEU SER ASN SER THR GLN SHEET 1 A 4 VAL A 3 SER A 4 0 SHEET 2 A 4 VAL A 64 LEU A 68 -1 O LEU A 65 N VAL A 3 SHEET 3 A 4 GLY A 46 VAL A 51 -1 N GLU A 50 O GLU A 67 SHEET 4 A 4 GLN A 21 ILE A 22 -1 N ILE A 22 O GLY A 46 SHEET 1 B 4 MET A 36 VAL A 41 0 SHEET 2 B 4 GLU A 27 SER A 33 -1 N VAL A 28 O ILE A 40 SHEET 3 B 4 GLY A 9 VAL A 14 -1 N ASN A 10 O GLU A 32 SHEET 4 B 4 PHE A 58 VAL A 59 -1 O VAL A 59 N GLY A 9 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 2 2 Bytes