Header list of 2hqi.pdb file
Complete list - r 9 2 Bytes
HEADER TRANSPORT 31-MAR-98 2HQI TITLE NMR SOLUTION STRUCTURE OF THE OXIDIZED FORM OF MERP, 14 STRUCTURES COMPND MOL_ID: 1; COMPND 2 MOLECULE: MERCURIC TRANSPORT PROTEIN; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: MERP; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SHIGELLA FLEXNERI; SOURCE 3 ORGANISM_TAXID: 623; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: BACTERIAL KEYWDS TRANSPORT, MERP, MERCURIC ION BINDING PROTEIN EXPDTA SOLUTION NMR NUMMDL 14 AUTHOR H.QIAN,L.SAHLMAN,P.O.ERIKSSON,C.HAMBREUS,U.EDLUND,I.SETHSON REVDAT 3 09-MAR-22 2HQI 1 REMARK REVDAT 2 24-FEB-09 2HQI 1 VERSN REVDAT 1 11-NOV-98 2HQI 0 JRNL AUTH H.QIAN,L.SAHLMAN,P.O.ERIKSSON,C.HAMBRAEUS,U.EDLUND,I.SETHSON JRNL TITL NMR SOLUTION STRUCTURE OF THE OXIDIZED FORM OF MERP, A JRNL TITL 2 MERCURIC ION BINDING PROTEIN INVOLVED IN BACTERIAL MERCURIC JRNL TITL 3 ION RESISTANCE. JRNL REF BIOCHEMISTRY V. 37 9316 1998 JRNL REFN ISSN 0006-2960 JRNL PMID 9649312 JRNL DOI 10.1021/BI9803628 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.8 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 2HQI COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL. REMARK 100 THE DEPOSITION ID IS D_1000178221. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 309 REMARK 210 PH : 4.9 REMARK 210 IONIC STRENGTH : 0.3 REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : WATER REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : UNITYPLUS REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : X-PLOR REMARK 210 METHOD USED : SA REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 20 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 14 REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL REMARK 210 REMARK 210 REMARK: TRIPLE RESONANCE EXPERIMENTS ON 13C, 15N-LABELED MERP 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 O GLN A 55 H LYS A 59 1.56 REMARK 500 H GLN A 3 O PHE A 47 1.57 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 1 PRO A 67 C - N - CD ANGL. DEV. = -14.1 DEGREES REMARK 500 2 PRO A 67 C - N - CD ANGL. DEV. = -15.3 DEGREES REMARK 500 3 PRO A 10 C - N - CD ANGL. DEV. = -18.5 DEGREES REMARK 500 3 PRO A 67 C - N - CD ANGL. DEV. = -13.3 DEGREES REMARK 500 4 PRO A 67 C - N - CD ANGL. DEV. = -18.0 DEGREES REMARK 500 5 PRO A 67 C - N - CD ANGL. DEV. = -17.2 DEGREES REMARK 500 6 PRO A 67 C - N - CD ANGL. DEV. = -18.6 DEGREES REMARK 500 7 PRO A 67 C - N - CD ANGL. DEV. = -17.6 DEGREES REMARK 500 8 PRO A 67 C - N - CD ANGL. DEV. = -12.9 DEGREES REMARK 500 9 PRO A 67 C - N - CD ANGL. DEV. = -16.2 DEGREES REMARK 500 10 PRO A 67 C - N - CD ANGL. DEV. = -17.1 DEGREES REMARK 500 11 PRO A 67 C - N - CD ANGL. DEV. = -17.1 DEGREES REMARK 500 12 PRO A 67 C - N - CD ANGL. DEV. = -18.2 DEGREES REMARK 500 13 PRO A 67 C - N - CD ANGL. DEV. = -14.7 DEGREES REMARK 500 14 PRO A 67 C - N - CD ANGL. DEV. = -17.6 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 THR A 2 175.35 -51.49 REMARK 500 1 VAL A 5 -167.03 -161.67 REMARK 500 1 PRO A 10 -162.13 -56.64 REMARK 500 1 MET A 12 -90.63 36.81 REMARK 500 1 ALA A 16 39.18 167.04 REMARK 500 1 VAL A 28 -159.11 -77.53 REMARK 500 1 VAL A 31 159.35 -41.11 REMARK 500 1 SER A 32 -50.96 -168.15 REMARK 500 1 ASP A 35 86.74 -164.82 REMARK 500 1 GLU A 39 -30.64 -39.23 REMARK 500 1 LYS A 40 -82.59 -137.10 REMARK 500 1 ARG A 41 61.48 169.60 REMARK 500 1 LYS A 51 13.67 -148.86 REMARK 500 1 ALA A 52 -154.16 -154.48 REMARK 500 1 PRO A 67 -155.87 -103.25 REMARK 500 2 VAL A 5 -167.46 -160.48 REMARK 500 2 PRO A 10 -164.14 -54.71 REMARK 500 2 MET A 12 -88.81 49.28 REMARK 500 2 CYS A 14 166.04 -43.88 REMARK 500 2 ALA A 15 60.08 -67.87 REMARK 500 2 ALA A 16 42.60 70.02 REMARK 500 2 LEU A 25 -73.56 -65.25 REMARK 500 2 VAL A 31 89.16 -46.43 REMARK 500 2 LYS A 40 -83.43 -138.69 REMARK 500 2 ARG A 41 62.32 171.20 REMARK 500 2 ASP A 48 51.10 -95.61 REMARK 500 2 ASP A 49 30.41 33.60 REMARK 500 2 LYS A 51 17.61 -168.44 REMARK 500 2 ALA A 52 -158.01 -174.71 REMARK 500 2 PRO A 67 -155.51 -105.87 REMARK 500 3 THR A 2 95.30 29.49 REMARK 500 3 MET A 12 100.45 50.67 REMARK 500 3 THR A 13 45.02 38.96 REMARK 500 3 ALA A 15 -46.68 81.88 REMARK 500 3 ALA A 16 29.09 -177.93 REMARK 500 3 LEU A 25 -70.27 -65.44 REMARK 500 3 VAL A 31 148.78 -30.96 REMARK 500 3 SER A 32 -50.34 -163.47 REMARK 500 3 LYS A 40 52.64 -168.41 REMARK 500 3 ARG A 41 42.66 31.55 REMARK 500 3 ASP A 49 53.23 -68.23 REMARK 500 3 LYS A 51 29.86 165.88 REMARK 500 3 ALA A 52 -168.73 -175.15 REMARK 500 3 PRO A 67 -157.45 -101.52 REMARK 500 4 THR A 2 74.77 -51.69 REMARK 500 4 GLN A 3 -169.20 -168.17 REMARK 500 4 PRO A 10 -160.75 -79.64 REMARK 500 4 MET A 12 -87.72 36.46 REMARK 500 4 ALA A 16 54.95 175.70 REMARK 500 4 LEU A 25 -71.49 -67.52 REMARK 500 REMARK 500 THIS ENTRY HAS 209 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL DBREF 2HQI A 1 72 UNP P04129 MERP_SHIFL 20 91 SEQRES 1 A 72 ALA THR GLN THR VAL THR LEU ALA VAL PRO GLY MET THR SEQRES 2 A 72 CYS ALA ALA CYS PRO ILE THR VAL LYS LYS ALA LEU SER SEQRES 3 A 72 LYS VAL GLU GLY VAL SER LYS VAL ASP VAL GLY PHE GLU SEQRES 4 A 72 LYS ARG GLU ALA VAL VAL THR PHE ASP ASP THR LYS ALA SEQRES 5 A 72 SER VAL GLN LYS LEU THR LYS ALA THR ALA ASP ALA GLY SEQRES 6 A 72 TYR PRO SER SER VAL LYS GLN HELIX 1 1 PRO A 18 LYS A 27 1 10 HELIX 2 2 VAL A 54 ALA A 62 1 9 SHEET 1 A 4 SER A 69 LYS A 71 0 SHEET 2 A 4 GLN A 3 ALA A 8 -1 N ALA A 8 O SER A 69 SHEET 3 A 4 GLU A 42 PHE A 47 -1 N PHE A 47 O GLN A 3 SHEET 4 A 4 LYS A 33 GLY A 37 -1 N GLY A 37 O GLU A 42 SSBOND 1 CYS A 14 CYS A 17 1555 1555 2.14 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