Header list of 1rdu.pdb file
Complete list - r 2 2 Bytes
HEADER BIOSYNTHETIC PROTEIN 06-NOV-03 1RDU TITLE NMR STRUCTURE OF A PUTATIVE NIFB PROTEIN FROM THERMOTOGA (TM1290), TITLE 2 WHICH BELONGS TO THE DUF35 FAMILY COMPND MOL_ID: 1; COMPND 2 MOLECULE: CONSERVED HYPOTHETICAL PROTEIN; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: THERMOTOGA MARITIMA; SOURCE 3 ORGANISM_TAXID: 2336; SOURCE 4 GENE: TM1290; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)RIL; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET25B KEYWDS ATNOS, CANDID, STRUCTURAL GENOMICS, JOINT CENTER FOR STRUCTURAL KEYWDS 2 GENOMICS, JCSG, PROTEIN STRUCTURE INITIATIVE, PSI, NITROGEN FIXATION KEYWDS 3 NIFB, BIOSYNTHETIC PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR T.ETEZADY-ESFARJANI,T.HERRMANN,W.PETI,H.E.KLOCK,S.A.LESLEY, AUTHOR 2 K.WUTHRICH,JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG) REVDAT 5 02-MAR-22 1RDU 1 REMARK REVDAT 4 28-JUL-10 1RDU 1 HEADER TITLE KEYWDS REVDAT 3 24-FEB-09 1RDU 1 VERSN REVDAT 2 18-JAN-05 1RDU 1 KEYWDS REMARK REVDAT 1 06-JUL-04 1RDU 0 JRNL AUTH T.ETEZADY-ESFARJANI,T.HERRMANN,W.PETI,H.E.KLOCK,S.A.LESLEY, JRNL AUTH 2 K.WUTHRICH,JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG) JRNL TITL NMR STRUCTURE DETERMINATION OF THE HYPOTHETICAL PROTEIN JRNL TITL 2 TM1290 FROM THERMOTOGA MARITIMA USING AUTOMATED NOESY JRNL TITL 3 ANALYSIS. JRNL REF J.BIOMOL.NMR V. 29 403 2004 JRNL REFN ISSN 0925-2738 JRNL PMID 15213441 JRNL DOI 10.1023/B:JNMR.0000032615.51536.1A REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : DYANA 6.0 REMARK 3 AUTHORS : GUENTERT REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1RDU COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-NOV-03. REMARK 100 THE DEPOSITION ID IS D_1000020671. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 313; 313 REMARK 210 PH : 6.0; 6.0 REMARK 210 IONIC STRENGTH : NULL; NULL REMARK 210 PRESSURE : NULL; NULL REMARK 210 SAMPLE CONTENTS : 2.3MM 15N-LABELED TM1290, 95% REMARK 210 H2O/5% D2O, 20MM SODIUM REMARK 210 PHOSPHATE, PH 6.0; 3.8MM 15N-13C- REMARK 210 LABELED TM1290, 95% H2O/5% D2O, REMARK 210 20MM SODIUM PHOSPHATE, PH 6.0 REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C REMARK 210 -SEPARATED_NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 900 MHZ REMARK 210 SPECTROMETER MODEL : AVANCE REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : XWINNMR 3.5, XEASY REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 80 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 2 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 REMARK 500 REMARK: NULL 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 65 CA - CB - CG ANGL. DEV. = 11.6 DEGREES REMARK 500 2 TYR A 65 CB - CG - CD2 ANGL. DEV. = -3.7 DEGREES REMARK 500 3 VAL A 94 CA - CB - CG2 ANGL. DEV. = 10.3 DEGREES REMARK 500 7 ARG A 3 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES REMARK 500 10 PHE A 112 CB - CG - CD1 ANGL. DEV. = -5.0 DEGREES REMARK 500 13 ARG A 3 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES REMARK 500 13 PHE A 112 CB - CG - CD2 ANGL. DEV. = -4.3 DEGREES REMARK 500 14 VAL A 4 CA - CB - CG1 ANGL. DEV. = 9.4 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 ASP A 19 38.80 -85.67 REMARK 500 1 ARG A 20 108.91 179.77 REMARK 500 1 THR A 32 43.29 -75.78 REMARK 500 1 GLU A 33 -37.72 -131.70 REMARK 500 1 HIS A 48 -174.72 61.59 REMARK 500 1 LYS A 53 -62.06 59.93 REMARK 500 1 VAL A 63 108.60 -53.46 REMARK 500 1 ARG A 73 -177.70 151.60 REMARK 500 1 ASN A 74 58.98 25.62 REMARK 500 1 ALA A 75 -29.30 -154.28 REMARK 500 1 LEU A 109 66.93 -103.51 REMARK 500 1 THR A 110 37.70 -96.03 REMARK 500 1 THR A 111 164.04 157.93 REMARK 500 1 ARG A 114 107.82 -164.17 REMARK 500 1 GLU A 115 38.38 -83.99 REMARK 500 2 ALA A 2 158.40 178.86 REMARK 500 2 LYS A 11 46.54 -93.48 REMARK 500 2 ASP A 19 38.44 -79.45 REMARK 500 2 ARG A 20 93.99 -172.61 REMARK 500 2 THR A 32 42.15 -88.16 REMARK 500 2 GLU A 33 -96.85 -130.33 REMARK 500 2 SER A 34 37.92 -95.72 REMARK 500 2 THR A 43 52.10 -101.65 REMARK 500 2 ALA A 47 39.67 -143.01 REMARK 500 2 LYS A 53 -63.56 63.51 REMARK 500 2 ARG A 73 -160.82 178.61 REMARK 500 2 ASN A 74 99.81 -28.93 REMARK 500 2 ALA A 75 -35.84 -175.98 REMARK 500 2 ALA A 82 36.61 -97.38 REMARK 500 2 GLU A 90 60.11 -154.31 REMARK 500 2 GLU A 103 35.62 -85.92 REMARK 500 2 ARG A 105 37.76 -98.34 REMARK 500 2 THR A 110 35.29 -91.25 REMARK 500 2 THR A 111 164.63 158.82 REMARK 500 2 PHE A 112 -169.65 -167.82 REMARK 500 2 ARG A 114 91.47 -162.67 REMARK 500 3 ASP A 19 38.59 -79.67 REMARK 500 3 ARG A 20 93.50 -163.46 REMARK 500 3 ARG A 23 38.29 -145.28 REMARK 500 3 GLU A 33 -34.67 -151.58 REMARK 500 3 SER A 34 38.03 -154.46 REMARK 500 3 THR A 43 62.22 -110.02 REMARK 500 3 HIS A 48 -47.28 -145.72 REMARK 500 3 THR A 50 87.76 52.10 REMARK 500 3 LYS A 53 -66.01 58.61 REMARK 500 3 ASN A 70 -177.89 -170.02 REMARK 500 3 ARG A 73 -86.02 164.52 REMARK 500 3 ALA A 75 -35.84 154.70 REMARK 500 3 GLU A 90 38.72 -150.45 REMARK 500 3 GLU A 103 35.65 -94.64 REMARK 500 REMARK 500 THIS ENTRY HAS 332 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 GLU A 115 GLY A 116 8 147.98 REMARK 500 ARG A 114 GLU A 115 13 147.28 REMARK 500 MET A 1 ALA A 2 14 140.09 REMARK 500 THR A 110 THR A 111 17 -148.68 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 2 ARG A 88 0.09 SIDE CHAIN REMARK 500 2 ARG A 105 0.09 SIDE CHAIN REMARK 500 4 TYR A 30 0.09 SIDE CHAIN REMARK 500 5 ARG A 23 0.09 SIDE CHAIN REMARK 500 5 PHE A 89 0.08 SIDE CHAIN REMARK 500 6 ARG A 73 0.09 SIDE CHAIN REMARK 500 6 ARG A 105 0.08 SIDE CHAIN REMARK 500 6 ARG A 114 0.15 SIDE CHAIN REMARK 500 8 ARG A 20 0.10 SIDE CHAIN REMARK 500 10 TYR A 26 0.07 SIDE CHAIN REMARK 500 10 PHE A 112 0.10 SIDE CHAIN REMARK 500 11 ARG A 114 0.08 SIDE CHAIN REMARK 500 12 TYR A 65 0.07 SIDE CHAIN REMARK 500 12 ARG A 105 0.09 SIDE CHAIN REMARK 500 12 ARG A 114 0.08 SIDE CHAIN REMARK 500 14 ARG A 114 0.09 SIDE CHAIN REMARK 500 15 TYR A 87 0.09 SIDE CHAIN REMARK 500 15 ARG A 105 0.09 SIDE CHAIN REMARK 500 16 ARG A 23 0.09 SIDE CHAIN REMARK 500 16 TYR A 65 0.08 SIDE CHAIN REMARK 500 17 ARG A 20 0.09 SIDE CHAIN REMARK 500 17 TYR A 65 0.07 SIDE CHAIN REMARK 500 18 ARG A 23 0.08 SIDE CHAIN REMARK 500 18 TYR A 30 0.09 SIDE CHAIN REMARK 500 18 TYR A 65 0.08 SIDE CHAIN REMARK 500 19 ARG A 20 0.12 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 283154 RELATED DB: TARGETDB DBREF 1RDU A 1 116 UNP Q9X116 Q9X116_THEMA 1 116 SEQRES 1 A 116 MET ALA ARG VAL ALA ILE PRO SER VAL GLY LYS ASP LEU SEQRES 2 A 116 SER SER MET VAL SER ASP ARG PHE ALA ARG ALA GLU TYR SEQRES 3 A 116 PHE ILE ILE TYR ASP THR GLU SER GLY ASN VAL GLU VAL SEQRES 4 A 116 VAL GLU ASN THR ILE ALA ASP ALA HIS GLY THR GLY PRO SEQRES 5 A 116 LYS VAL VAL GLN SER LEU VAL SER LYS GLY VAL GLU TYR SEQRES 6 A 116 LEU ILE ALA SER ASN VAL GLY ARG ASN ALA PHE GLU THR SEQRES 7 A 116 LEU LYS ALA ALA GLY VAL LYS VAL TYR ARG PHE GLU GLY SEQRES 8 A 116 GLY THR VAL GLN GLU ALA ILE ASP ALA PHE SER GLU GLY SEQRES 9 A 116 ARG LEU GLU GLU LEU THR THR PHE THR ARG GLU GLY HELIX 1 1 ARG A 20 ALA A 24 5 5 HELIX 2 2 LYS A 53 SER A 60 1 8 HELIX 3 3 ALA A 75 ALA A 81 1 7 HELIX 4 4 THR A 93 GLU A 103 1 11 SHEET 1 A 5 VAL A 37 GLU A 41 0 SHEET 2 A 5 TYR A 26 ASP A 31 -1 N PHE A 27 O VAL A 40 SHEET 3 A 5 ARG A 3 SER A 8 -1 N SER A 8 O TYR A 26 SHEET 4 A 5 TYR A 65 ILE A 67 1 O ILE A 67 N ALA A 5 SHEET 5 A 5 LYS A 85 TYR A 87 1 O TYR A 87 N LEU A 66 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