Header list of 2g0u.pdb file
Complete list - r 9 2 Bytes
HEADER UNKNOWN FUNCTION 13-FEB-06 2G0U TITLE SOLUTION STRUCTURE OF MONOMERIC BSAL, THE TYPE III SECRETION NEEDLE TITLE 2 PROTEIN OF BURKHOLDERIA PSEUDOMALLEI COMPND MOL_ID: 1; COMPND 2 MOLECULE: TYPE III SECRETION SYSTEM NEEDLE PROTEIN; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: BSALDELTA5; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: BURKHOLDERIA PSEUDOMALLEI; SOURCE 3 ORGANISM_TAXID: 28450; SOURCE 4 STRAIN: E264; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS HELIX-TURN-HELIX, UNKNOWN FUNCTION EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR L.ZHANG,Y.WANG,W.L.PICKING,W.D.PICKING,R.N.DE GUZMAN REVDAT 3 09-MAR-22 2G0U 1 REMARK SEQADV REVDAT 2 24-FEB-09 2G0U 1 VERSN REVDAT 1 23-MAY-06 2G0U 0 JRNL AUTH L.ZHANG,Y.WANG,W.L.PICKING,W.D.PICKING,R.N.DE GUZMAN JRNL TITL SOLUTION STRUCTURE OF MONOMERIC BSAL, THE TYPE III SECRETION JRNL TITL 2 NEEDLE PROTEIN OF BURKHOLDERIA PSEUDOMALLEI. JRNL REF J.MOL.BIOL. V. 359 322 2006 JRNL REFN ISSN 0022-2836 JRNL PMID 16631790 JRNL DOI 10.1016/J.JMB.2006.03.028 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : NMRPIPE 2005, CYANA, AMBER 7 REMARK 3 AUTHORS : DELAGLIO, F., GRZESIEK, S., VUISTER, G.W., ZHU, REMARK 3 G., PFEIFER, J., AND BAX, A. (NMRPIPE), GUNTERT, REMARK 3 P. (CYANA), CASE, D.A., PEARLMAN, D.A., CALDWELL, REMARK 3 J.W., CHEATHAM III, T.E., WANG, J., ROSS, W.S., REMARK 3 SIMMERLING, C.L., DARDEN, T.A., MERZ, K.M., REMARK 3 STANTON, R.V., CHENG, A.L., VINCENT, J.J., CROWLEY, REMARK 3 M., TSUI, V., GOHLKE, H., RADMER, R.J., DUAN, Y., REMARK 3 PITERA, J., MASSOVA, I., SEIBEL, G.L., SINGH, U.C., REMARK 3 WEINER, P.K., AND KOLLMAN, P.A. (AMBER) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 2G0U COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-FEB-06. REMARK 100 THE DEPOSITION ID IS D_1000036546. 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 : 20MM REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C REMARK 210 -SEPARATED_NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 600 MHZ REMARK 210 SPECTROMETER MODEL : AVANCE; INOVA REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRVIEW 5.0.2 REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS SIMULATED REMARK 210 ANNEALING MOLECULAR DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 200 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST REMARK 210 RESTRAINT VIOLATIONS,STRUCTURES REMARK 210 WITH THE LOWEST ENERGY 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 3 ARG A 23 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES REMARK 500 4 ARG A 23 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES REMARK 500 10 ARG A 23 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES REMARK 500 11 ARG A 23 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES REMARK 500 17 ARG A 23 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES REMARK 500 18 ARG A 23 NE - CZ - NH1 ANGL. DEV. = 3.2 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 LEU A 8 14.22 -144.85 REMARK 500 1 ALA A 10 28.75 -141.43 REMARK 500 1 GLU A 13 -40.90 -159.65 REMARK 500 1 ASP A 26 18.16 -144.09 REMARK 500 1 ASN A 46 86.80 -152.71 REMARK 500 1 HIS A 90 -50.10 -136.24 REMARK 500 2 TYR A 12 13.44 -61.15 REMARK 500 2 THR A 19 -164.42 -165.46 REMARK 500 2 ALA A 24 -44.02 -141.21 REMARK 500 2 LEU A 85 37.76 -76.72 REMARK 500 2 HIS A 88 23.75 -68.44 REMARK 500 3 PRO A 5 157.18 -48.59 REMARK 500 3 ASP A 26 2.93 -67.98 REMARK 500 3 ASN A 46 89.89 -151.23 REMARK 500 3 SER A 83 -8.71 -140.78 REMARK 500 5 LEU A 9 14.35 -66.52 REMARK 500 5 ASP A 26 -43.61 -139.73 REMARK 500 5 ASN A 46 86.49 -151.24 REMARK 500 6 TRP A 14 28.55 -66.09 REMARK 500 6 VAL A 29 -47.33 -146.62 REMARK 500 6 ILE A 84 -11.91 -145.18 REMARK 500 7 TRP A 14 28.55 -66.09 REMARK 500 7 VAL A 29 -47.33 -146.62 REMARK 500 7 ILE A 84 -11.91 -145.18 REMARK 500 8 ALA A 10 -6.28 -154.25 REMARK 500 8 SER A 15 109.92 -57.11 REMARK 500 8 THR A 19 29.52 -148.68 REMARK 500 8 ILE A 21 71.01 0.01 REMARK 500 9 LEU A 9 -2.39 -144.56 REMARK 500 9 ARG A 23 -20.59 -145.78 REMARK 500 9 SER A 76 19.55 -140.74 REMARK 500 9 SER A 83 -1.94 -142.50 REMARK 500 9 HIS A 91 -3.86 -147.58 REMARK 500 10 GLU A 13 -41.59 -154.00 REMARK 500 10 ASN A 46 89.89 -151.25 REMARK 500 11 HIS A 87 -49.39 -150.81 REMARK 500 11 HIS A 91 10.74 -150.19 REMARK 500 12 PRO A 7 108.37 -52.08 REMARK 500 12 TYR A 12 -7.93 -55.18 REMARK 500 12 TRP A 14 -24.63 -151.34 REMARK 500 12 ILE A 21 118.50 -25.73 REMARK 500 13 THR A 6 151.93 66.76 REMARK 500 13 ASP A 11 -44.77 -159.08 REMARK 500 13 SER A 83 31.09 -152.12 REMARK 500 13 HIS A 89 39.51 -73.64 REMARK 500 14 GLU A 13 -4.36 -142.51 REMARK 500 14 ASN A 46 87.77 -151.77 REMARK 500 14 ILE A 84 42.22 -77.72 REMARK 500 15 PRO A 7 -4.29 -58.74 REMARK 500 15 ALA A 10 22.92 -144.45 REMARK 500 REMARK 500 THIS ENTRY HAS 63 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 TYR A 56 0.10 SIDE CHAIN REMARK 500 2 TYR A 56 0.09 SIDE CHAIN REMARK 500 3 TYR A 56 0.10 SIDE CHAIN REMARK 500 4 TYR A 56 0.08 SIDE CHAIN REMARK 500 4 TYR A 63 0.06 SIDE CHAIN REMARK 500 5 TYR A 56 0.09 SIDE CHAIN REMARK 500 6 TYR A 56 0.10 SIDE CHAIN REMARK 500 7 TYR A 56 0.10 SIDE CHAIN REMARK 500 8 TYR A 56 0.07 SIDE CHAIN REMARK 500 9 TYR A 56 0.08 SIDE CHAIN REMARK 500 10 TYR A 56 0.08 SIDE CHAIN REMARK 500 11 TYR A 56 0.09 SIDE CHAIN REMARK 500 12 TYR A 56 0.08 SIDE CHAIN REMARK 500 13 TYR A 56 0.07 SIDE CHAIN REMARK 500 14 TYR A 56 0.08 SIDE CHAIN REMARK 500 15 TYR A 56 0.08 SIDE CHAIN REMARK 500 16 TYR A 56 0.10 SIDE CHAIN REMARK 500 17 TYR A 56 0.08 SIDE CHAIN REMARK 500 18 TYR A 56 0.08 SIDE CHAIN REMARK 500 19 TYR A 56 0.09 SIDE CHAIN REMARK 500 20 TYR A 56 0.10 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL DBREF 2G0U A 1 84 UNP Q63K18 Q63K18_BURPS 1 84 SEQADV 2G0U ALA A 10 UNP Q63K18 THR 10 CONFLICT SEQADV 2G0U ASP A 27 UNP Q63K18 THR 27 CONFLICT SEQADV 2G0U LYS A 34 UNP Q63K18 GLN 34 CONFLICT SEQADV 2G0U LEU A 85 UNP Q63K18 EXPRESSION TAG SEQADV 2G0U GLU A 86 UNP Q63K18 EXPRESSION TAG SEQADV 2G0U HIS A 87 UNP Q63K18 EXPRESSION TAG SEQADV 2G0U HIS A 88 UNP Q63K18 EXPRESSION TAG SEQADV 2G0U HIS A 89 UNP Q63K18 EXPRESSION TAG SEQADV 2G0U HIS A 90 UNP Q63K18 EXPRESSION TAG SEQADV 2G0U HIS A 91 UNP Q63K18 EXPRESSION TAG SEQADV 2G0U HIS A 92 UNP Q63K18 EXPRESSION TAG SEQRES 1 A 92 MET SER ASN PRO PRO THR PRO LEU LEU ALA ASP TYR GLU SEQRES 2 A 92 TRP SER GLY TYR LEU THR GLY ILE GLY ARG ALA PHE ASP SEQRES 3 A 92 ASP GLY VAL LYS ASP LEU ASN LYS GLN LEU GLN ASP ALA SEQRES 4 A 92 GLN ALA ASN LEU THR LYS ASN PRO SER ASP PRO THR ALA SEQRES 5 A 92 LEU ALA ASN TYR GLN MET ILE MET SER GLU TYR ASN LEU SEQRES 6 A 92 TYR ARG ASN ALA GLN SER SER ALA VAL LYS SER MET LYS SEQRES 7 A 92 ASP ILE ASP SER SER ILE LEU GLU HIS HIS HIS HIS HIS SEQRES 8 A 92 HIS HELIX 1 1 SER A 15 ARG A 23 1 9 HELIX 2 2 ALA A 24 ASP A 26 5 3 HELIX 3 3 VAL A 29 ASN A 46 1 18 HELIX 4 4 ASP A 49 SER A 76 1 28 HELIX 5 5 SER A 76 ASP A 81 1 6 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 9 2 Bytes