Header list of 1qq3.pdb file
Complete list - 3 20 Bytes
HEADER ELECTRON TRANSPORT 10-JUN-99 1QQ3 TITLE THE SOLUTION STRUCTURE OF THE HEME BINDING VARIANT ARG98CYS OF TITLE 2 OXIDIZED ESCHERICHIA COLI CYTOCHROME B562 COMPND MOL_ID: 1; COMPND 2 MOLECULE: CYTOCHROME B562; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI; SOURCE 3 ORGANISM_TAXID: 562; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PCEB562 KEYWDS FOUR HELIX BUNDLE, HEMOPROTEIN, ELECTRON TRANSPORT EXPDTA SOLUTION NMR MDLTYP MINIMIZED AVERAGE AUTHOR F.ARNESANO,L.BANCI,I.BERTINI,S.CIOFI-BAFFONI,P.D.BARKER,T.WOODYEAR REVDAT 4 03-NOV-21 1QQ3 1 REMARK SEQADV LINK REVDAT 3 24-FEB-09 1QQ3 1 VERSN REVDAT 2 01-APR-03 1QQ3 1 JRNL REVDAT 1 24-MAY-00 1QQ3 0 JRNL AUTH F.ARNESANO,L.BANCI,I.BERTINI,S.CIOFI-BAFFONI,T.L.WOODYEAR, JRNL AUTH 2 C.M.JOHNSON,P.D.BARKER JRNL TITL STRUCTURAL CONSEQUENCES OF B- TO C-TYPE HEME CONVERSION IN JRNL TITL 2 OXIDIZED ESCHERICHIA COLI CYTOCHROME B562. JRNL REF BIOCHEMISTRY V. 39 1499 2000 JRNL REFN ISSN 0006-2960 JRNL PMID 10684632 JRNL DOI 10.1021/BI991831O REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR, AMBER 5.0 REMARK 3 AUTHORS : PEARLMAN, D.A., CASE, D.A., CALDWELL, J.W., ROSS, REMARK 3 W.S., CHEATHAM, T.E., FERGUSON, D.M., SEIBEL, G.L., REMARK 3 SINGH, U.C., WEINER, P.K., & KOLLMAN, P.A. (AMBER) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: A TOTAL OF 4325 NOESY CROSS-PEAKS WAS REMARK 3 ASSIGNED, INTEGRATED AND TRANSFORMED IN UPPER DISTANCE LIMITS; REMARK 3 23 DISTANCE CONSTRAINTS WERE DERIVED FROM 1D NOE EXPERIMENTS REMARK 3 INVOLVING FAST RELAXING PARAMAGNETIC SHIFTED SIGNALS. TOTALLY, REMARK 3 THEY CORRESPONDED TO 2595 UPPER DISTANCE LIMITS, OF WHICH 2145 REMARK 3 WERE FOUND TO BE MEANINGFUL. IN ADDITION, 45 3JHNHA COUPLINGS REMARK 3 OBTAINED FROM THE HNHA 3D SPECTRUM AND 397 PCS WERE USED FOR THE REMARK 3 STRUCTURE CALCULATIONS. REMARK 4 REMARK 4 1QQ3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-JUN-99. REMARK 100 THE DEPOSITION ID IS D_1000009166. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298; 298 REMARK 210 PH : 4.8; 4.8 REMARK 210 IONIC STRENGTH : 500MM PHOSPHATE; 500MM PHOSPHATE REMARK 210 PRESSURE : AMBIENT; AMBIENT REMARK 210 SAMPLE CONTENTS : 3MM R98C CYTOCHROME B562; 500MM REMARK 210 PHOSPHATE BUFFER; 90% H2O, 10% REMARK 210 D2O; 2.5MM R98C CYTOCHROME B562; REMARK 210 500MM PHOSPHATE BUFFER; 90% H2O, REMARK 210 10% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D_15N REMARK 210 -SEPARATED_NOESY; HNHA; 1D NOE REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 600 MHZ REMARK 210 SPECTROMETER MODEL : AVANCE REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : DYANA 1.5, XEASY, PSEUDODYANA REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS FOLLOWED REMARK 210 BY ENERGY MINIMIZATION REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1 REMARK 210 CONFORMERS, SELECTION CRITERIA : ENERGY MINIMIZED AVERAGE REMARK 210 STRUCTURE REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL 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 HB1 ALA A 1 OD2 ASP A 39 1.57 REMARK 500 CB ALA A 1 OD2 ASP A 39 1.99 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS 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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) 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 RES CSSEQI ATM2 DEVIATION REMARK 500 ALA A 1 CA ALA A 1 CB -0.436 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 ASP A 21 -39.58 -132.59 REMARK 500 PRO A 56 20.71 -75.18 REMARK 500 REMARK 500 REMARK: NULL REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 HEB A 107 FE REMARK 620 N RES CSSEQI ATOM REMARK 620 1 MET A 7 SD REMARK 620 2 HEB A 107 NA 84.0 REMARK 620 3 HEB A 107 NB 98.6 90.1 REMARK 620 4 HEB A 107 NC 95.4 177.6 92.3 REMARK 620 5 HEB A 107 ND 81.2 90.6 179.2 87.0 REMARK 620 6 HIS A 102 NE2 171.3 87.5 82.9 93.1 97.4 REMARK 620 N 1 2 3 4 5 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEB A 107 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1QPU RELATED DB: PDB REMARK 900 1QPU CONTAINS THE SOLUTION STRUCTURE OF WILD-TYPE OXIDIZED REMARK 900 ESCHERICHIA COLI CYTOCHROME B562 DBREF 1QQ3 A 1 106 UNP P0ABE7 C562_ECOLI 23 128 SEQADV 1QQ3 CYS A 98 UNP P0ABE7 ARG 120 ENGINEERED MUTATION SEQRES 1 A 106 ALA ASP LEU GLU ASP ASN MET GLU THR LEU ASN ASP ASN SEQRES 2 A 106 LEU LYS VAL ILE GLU LYS ALA ASP ASN ALA ALA GLN VAL SEQRES 3 A 106 LYS ASP ALA LEU THR LYS MET ARG ALA ALA ALA LEU ASP SEQRES 4 A 106 ALA GLN LYS ALA THR PRO PRO LYS LEU GLU ASP LYS SER SEQRES 5 A 106 PRO ASP SER PRO GLU MET LYS ASP PHE ARG HIS GLY PHE SEQRES 6 A 106 ASP ILE LEU VAL GLY GLN ILE ASP ASP ALA LEU LYS LEU SEQRES 7 A 106 ALA ASN GLU GLY LYS VAL LYS GLU ALA GLN ALA ALA ALA SEQRES 8 A 106 GLU GLN LEU LYS THR THR CYS ASN ALA TYR HIS GLN LYS SEQRES 9 A 106 TYR ARG HET HEB A 107 74 HETNAM HEB HEME B/C HETSYN HEB HYBRID BETWEEN B AND C TYPE HEMES (PROTOPORPHYRIN IX HETSYN 2 HEB CONTAINING FE) FORMUL 2 HEB C34 H34 FE N4 O4 HELIX 1 1 ASP A 2 LYS A 19 1 18 HELIX 2 2 ASN A 22 GLN A 41 1 20 HELIX 3 3 PRO A 45 GLU A 49 5 5 HELIX 4 4 GLU A 57 GLU A 81 1 25 HELIX 5 5 LYS A 83 GLN A 103 1 21 LINK SG CYS A 98 CAB HEB A 107 1555 1555 1.78 LINK SD MET A 7 FE HEB A 107 1555 1555 2.32 LINK NE2 HIS A 102 FE HEB A 107 1555 1555 2.00 SITE 1 AC1 12 MET A 7 LEU A 14 PRO A 45 PRO A 46 SITE 2 AC1 12 PHE A 61 GLY A 64 PHE A 65 LEU A 68 SITE 3 AC1 12 CYS A 98 HIS A 102 TYR A 105 ARG A 106 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
Complete list - 3 20 Bytes