Header list of 2gdw.pdb file
Complete list - v 10 2 Bytes
HEADER LIGASE/TRANSPORT PROTEIN 17-MAR-06 2GDW TITLE SOLUTION STRUCTURE OF THE B. BREVIS TYCC3-PCP IN A/H-STATE COMPND MOL_ID: 1; COMPND 2 MOLECULE: TYROCIDINE SYNTHETASE III; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: ACYL CARRIER 3, TYCC3 THIOESTER DOMAIN; COMPND 5 SYNONYM: NON-RIBOSOMAL PEPTIDE SYNTHETASE PEPTIDYL CARRIER PROTEIN; COMPND 6 ENGINEERED: YES; COMPND 7 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: BREVIBACILLUS PARABREVIS; SOURCE 3 ORGANISM_TAXID: 54914; SOURCE 4 STRAIN: ATCC8185; SOURCE 5 GENE: TYCC; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: XL10; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PQE70 KEYWDS THREE-HELIX BUNDLE, LIGASE-TRANSPORT PROTEIN COMPLEX EXPDTA SOLUTION NMR NUMMDL 19 AUTHOR A.KOGLIN,F.LOEHR,V.V.ROGOV,M.A.MARAHIEL,F.BERNHARD,V.DOETSCH REVDAT 3 10-NOV-21 2GDW 1 REMARK SEQADV REVDAT 2 24-FEB-09 2GDW 1 VERSN REVDAT 1 01-AUG-06 2GDW 0 JRNL AUTH A.KOGLIN,M.R.MOFID,F.LOEHR,B.SCHAEFER,V.V.ROGOV,M.-M.BLUM, JRNL AUTH 2 T.MITTAG,M.A.MARAHIEL,F.BERNHARD,V.DOETSCH JRNL TITL CONFORMATIONAL SWITCHES MODULATE PROTEIN INTERACTIONS IN JRNL TITL 2 PEPTIDE ANTIBIOTIC SYNTHETASES JRNL REF SCIENCE V. 312 273 2006 JRNL REFN ISSN 0036-8075 JRNL PMID 16614225 JRNL DOI 10.1126/SCIENCE.1122928 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 2.6, GROMOS 97 REMARK 3 AUTHORS : BRUKER (XWINNMR), VAN GUNSTEREN (GROMOS) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 2GDW COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-MAR-06. REMARK 100 THE DEPOSITION ID IS D_1000036997. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 6.8 REMARK 210 IONIC STRENGTH : 50MM NAPI; 1MM TCEP REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : 0.8MM A/H-PCP U-15N; 50MM NAPI; REMARK 210 1MM TCEP; 95% H2O; 5% D2O; 0.8MM REMARK 210 A/H-PCP; 50MM NAPI; 100% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 2D NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 900 MHZ; 800 MHZ REMARK 210 SPECTROMETER MODEL : AVANCE REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : XWINNMR 2.6, SPARKY 3.111, DYANA REMARK 210 1.5 REMARK 210 METHOD USED : ENERGY MINIMIZATION REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 19 REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION 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 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 2 TYR A 59 CB - CG - CD2 ANGL. DEV. = -3.6 DEGREES REMARK 500 6 TYR A 59 CB - CG - CD2 ANGL. DEV. = -3.8 DEGREES REMARK 500 17 TYR A 59 CB - CG - CD2 ANGL. DEV. = -4.0 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 VAL A 3 130.85 62.84 REMARK 500 1 GLU A 5 -166.11 -125.11 REMARK 500 1 TYR A 8 -60.56 177.20 REMARK 500 1 VAL A 9 79.29 57.33 REMARK 500 1 PRO A 11 -152.16 -70.76 REMARK 500 1 THR A 12 -83.15 -162.82 REMARK 500 1 VAL A 29 90.43 -13.83 REMARK 500 1 SER A 30 -69.37 -141.89 REMARK 500 1 ASP A 36 -154.06 54.46 REMARK 500 1 PHE A 38 5.38 37.56 REMARK 500 1 PHE A 39 -79.25 -116.38 REMARK 500 1 SER A 45 -146.92 -163.59 REMARK 500 1 HIS A 56 -77.92 -69.24 REMARK 500 1 LEU A 65 -46.87 60.98 REMARK 500 1 GLN A 71 61.93 -119.57 REMARK 500 1 PRO A 72 38.17 -79.87 REMARK 500 1 ALA A 82 56.13 -116.42 REMARK 500 1 THR A 83 -65.55 -162.35 REMARK 500 2 VAL A 3 -51.25 171.43 REMARK 500 2 THR A 4 -144.59 -176.09 REMARK 500 2 GLN A 7 -99.51 -168.58 REMARK 500 2 VAL A 9 71.46 56.25 REMARK 500 2 PRO A 11 -154.89 -68.75 REMARK 500 2 THR A 12 -85.86 -159.73 REMARK 500 2 VAL A 29 87.94 -10.45 REMARK 500 2 SER A 30 -50.66 -139.19 REMARK 500 2 ASP A 36 -163.48 56.96 REMARK 500 2 PHE A 38 -38.33 53.97 REMARK 500 2 PHE A 39 -81.57 -73.09 REMARK 500 2 GLN A 40 21.98 -73.19 REMARK 500 2 HIS A 44 46.63 -82.55 REMARK 500 2 SER A 45 -150.51 -150.48 REMARK 500 2 GLN A 60 -36.39 65.69 REMARK 500 2 LEU A 65 -43.96 62.37 REMARK 500 2 ALA A 82 50.90 -112.87 REMARK 500 2 THR A 83 -55.11 -160.26 REMARK 500 3 VAL A 3 78.32 -12.94 REMARK 500 3 GLU A 5 -174.56 -61.09 REMARK 500 3 ALA A 6 -71.33 67.43 REMARK 500 3 GLN A 7 -56.46 46.38 REMARK 500 3 TYR A 8 -65.45 -175.99 REMARK 500 3 VAL A 9 95.75 57.99 REMARK 500 3 THR A 12 -80.31 -113.33 REMARK 500 3 VAL A 29 79.70 1.62 REMARK 500 3 ASP A 36 -156.03 58.77 REMARK 500 3 PHE A 38 34.27 36.87 REMARK 500 3 PHE A 39 -81.42 -152.49 REMARK 500 3 GLN A 40 29.91 -70.94 REMARK 500 3 HIS A 44 45.95 -93.05 REMARK 500 3 SER A 45 -159.76 -174.94 REMARK 500 REMARK 500 THIS ENTRY HAS 363 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 3 TYR A 80 0.07 SIDE CHAIN REMARK 500 6 HIS A 44 0.11 SIDE CHAIN REMARK 500 6 TYR A 80 0.07 SIDE CHAIN REMARK 500 7 HIS A 44 0.11 SIDE CHAIN REMARK 500 9 TYR A 59 0.06 SIDE CHAIN REMARK 500 11 PHE A 39 0.08 SIDE CHAIN REMARK 500 11 TYR A 80 0.06 SIDE CHAIN REMARK 500 12 PHE A 39 0.08 SIDE CHAIN REMARK 500 12 TYR A 59 0.07 SIDE CHAIN REMARK 500 12 TYR A 80 0.07 SIDE CHAIN REMARK 500 13 TYR A 59 0.07 SIDE CHAIN REMARK 500 14 TYR A 80 0.07 SIDE CHAIN REMARK 500 15 TYR A 8 0.08 SIDE CHAIN REMARK 500 15 PHE A 39 0.08 SIDE CHAIN REMARK 500 17 TYR A 8 0.07 SIDE CHAIN REMARK 500 18 TYR A 8 0.14 SIDE CHAIN REMARK 500 19 TYR A 80 0.17 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY REMARK 500 REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 500 I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI ANGLE REMARK 500 4 GLY A 43 -10.96 REMARK 500 5 LYS A 66 -10.72 REMARK 500 7 PHE A 39 -10.71 REMARK 500 12 LYS A 66 -10.83 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 2GDX RELATED DB: PDB REMARK 900 SOLUTION STRUCTURE OF THE B. BREVIS TYCC3-PCP IN H-STATE REMARK 900 RELATED ID: 2GDY RELATED DB: PDB REMARK 900 SOLUTION STRUCTURE OF THE B. BREVIS TYCC3-PCP IN A-STATE REMARK 900 RELATED ID: 2GE1 RELATED DB: PDB REMARK 900 PROTEIN COMPLEX OF A-STATE TYCC3-APO-PCP WITH THE PPTASE SFP (MODEL) REMARK 900 RELATED ID: 2GE0 RELATED DB: PDB REMARK 900 ACTIVE COMPLEX OF COENZYME A WITH THE PPTASE SFP (MODEL) DBREF 2GDW A 2 83 UNP O30409 TYCC_BREPA 3032 3113 SEQADV 2GDW MET A 1 UNP O30409 INITIATING METHIONINE SEQADV 2GDW GLY A 2 UNP O30409 PRO 3032 ENGINEERED MUTATION SEQADV 2GDW ARG A 84 UNP O30409 CLONING ARTIFACT SEQADV 2GDW SER A 85 UNP O30409 CLONING ARTIFACT SEQRES 1 A 85 MET GLY VAL THR GLU ALA GLN TYR VAL ALA PRO THR ASN SEQRES 2 A 85 ALA VAL GLU SER LYS LEU ALA GLU ILE TRP GLU ARG VAL SEQRES 3 A 85 LEU GLY VAL SER GLY ILE GLY ILE LEU ASP ASN PHE PHE SEQRES 4 A 85 GLN ILE GLY GLY HIS SER LEU LYS ALA MET ALA VAL ALA SEQRES 5 A 85 ALA GLN VAL HIS ARG GLU TYR GLN VAL GLU LEU PRO LEU SEQRES 6 A 85 LYS VAL LEU PHE ALA GLN PRO THR ILE LYS ALA LEU ALA SEQRES 7 A 85 GLN TYR VAL ALA THR ARG SER HELIX 1 1 ASN A 13 LEU A 27 1 15 HELIX 2 2 SER A 45 GLU A 58 1 14 HELIX 3 3 LEU A 65 GLN A 71 1 7 HELIX 4 4 THR A 73 ALA A 82 1 10 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 - v 10 2 Bytes