Header list of 1kwj.pdb file
Complete list - 27 20 Bytes
HEADER OXYGEN STORAGE/TRANSPORT 29-JAN-02 1KWJ TITLE SOLUTION STRUCTURE DETERMINATION OF THE FULLY OXIDIZED DOUBLE MUTANT TITLE 2 K9-10A CYTOCHROME C7 FROM DESULFUROMONAS ACETOXIDANS, MINIMIZED TITLE 3 AVERAGE STRUCTURE CAVEAT 1KWJ CHIRALITY ERROR AT CA CENTER OF ALA A 1 COMPND MOL_ID: 1; COMPND 2 MOLECULE: CYTOCHROME C7; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: CYTOCHROME C3, CYTOCHROME C551.5; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: DESULFUROMONAS ACETOXIDANS; SOURCE 3 ORGANISM_TAXID: 891; SOURCE 4 EXPRESSION_SYSTEM: DESULFOVIBRIO DESULFURICANS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 876; SOURCE 6 EXPRESSION_SYSTEM_STRAIN: G201 KEYWDS AUTOMATIC ASSIGNMENT, CYTOCHROME C7, ELECTRON TRANSFER, MULTIHEME KEYWDS 2 CYTOCHROMES, NMR SOLUTION STRUCTURE, OXYGEN STORAGE-TRANSPORT KEYWDS 3 COMPLEX EXPDTA SOLUTION NMR AUTHOR M.ASSFALG,I.BERTINI,P.TURANO,M.BRUSCHI,M.C.DURAND,M.T.GIUDICI- AUTHOR 2 ORTICONI,A.DOLLA REVDAT 4 27-OCT-21 1KWJ 1 REMARK SEQADV LINK REVDAT 3 24-FEB-09 1KWJ 1 VERSN REVDAT 2 13-MAR-02 1KWJ 1 JRNL REMARK TITLE REVDAT 1 06-FEB-02 1KWJ 0 JRNL AUTH M.ASSFALG,I.BERTINI,P.TURANO,M.BRUSCHI,M.C.DURAND, JRNL AUTH 2 M.T.GIUDICI-ORTICONI,A.DOLLA JRNL TITL A QUICK SOLUTION STRUCTURE DETERMINATION OF THE FULLY JRNL TITL 2 OXIDIZED DOUBLE MUTANT K9-10A CYTOCHROME C7 FROM JRNL TITL 3 DESULFUROMONAS ACETOXIDANS AND MECHANISTIC IMPLICATIONS. JRNL REF J.BIOMOL.NMR V. 22 107 2002 JRNL REFN ISSN 0925-2738 JRNL PMID 11883773 JRNL DOI 10.1023/A:1014202405862 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PSEUDYANA 1.5, AMBER 5.0 REMARK 3 AUTHORS : GUENTERT, P., WUETHRICH, K. (PSEUDYANA), KOLMAN, REMARK 3 CASE (AMBER) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1KWJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-JAN-02. REMARK 100 THE DEPOSITION ID IS D_1000015409. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 6.5 REMARK 210 IONIC STRENGTH : 100 MM PHOSPHATE REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 2MM CYTOCHROME C7, 100 MM SODIUM REMARK 210 PHOSPHATE BUFFER, PH 6.5 REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ REMARK 210 SPECTROMETER MODEL : AVANCE REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NULL REMARK 210 METHOD USED : SIMULATED ANNEALING IN TORSION REMARK 210 ANGLE SPACE; RESTRAINED ENERGY REMARK 210 MINIMIZATION REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1 REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL 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: 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 2 -133.56 -82.30 REMARK 500 THR A 14 93.29 63.53 REMARK 500 LYS A 18 -75.21 -67.02 REMARK 500 CYS A 26 -59.51 62.48 REMARK 500 GLU A 31 82.01 -66.35 REMARK 500 ASP A 47 -59.40 -148.84 REMARK 500 CYS A 49 -62.33 67.60 REMARK 500 ASN A 56 -168.67 -128.56 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 HEC A 130 FE REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS A 17 NE2 REMARK 620 2 HEC A 130 NA 91.4 REMARK 620 3 HEC A 130 NB 92.4 92.8 REMARK 620 4 HEC A 130 NC 88.4 177.6 89.6 REMARK 620 5 HEC A 130 ND 87.3 88.5 178.7 89.1 REMARK 620 6 HIS A 30 NE2 175.4 92.7 89.6 87.4 90.7 REMARK 620 N 1 2 3 4 5 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 HEC A 153 FE REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS A 20 NE2 REMARK 620 2 HEC A 153 NA 91.1 REMARK 620 3 HEC A 153 NB 91.7 89.8 REMARK 620 4 HEC A 153 NC 89.5 179.1 90.8 REMARK 620 5 HEC A 153 ND 87.0 90.5 178.6 88.9 REMARK 620 6 HIS A 53 NE2 177.4 90.3 90.5 89.1 90.8 REMARK 620 N 1 2 3 4 5 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 HEC A 166 FE REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS A 45 NE2 REMARK 620 2 HEC A 166 NA 91.8 REMARK 620 3 HEC A 166 NB 89.6 91.3 REMARK 620 4 HEC A 166 NC 91.2 176.9 89.0 REMARK 620 5 HEC A 166 ND 89.1 90.2 178.1 89.6 REMARK 620 6 HIS A 66 NE2 177.3 88.1 93.0 88.9 88.2 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 HEC A 130 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC A 153 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC A 166 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1EHJ RELATED DB: PDB REMARK 900 1EHJ CONTAINS THE ENERGY MINIMIZED AVERAGE SOLUTION STRUCTURE OF REMARK 900 THE FULLY REDUCED NATIVE CYTOCHROME C7 FROM DESULFUROMONAS REMARK 900 ACETOXIDANS REMARK 900 RELATED ID: 1F22 RELATED DB: PDB REMARK 900 1F22 CONTAINS THE 35 SOLUTION STRUCTURES FAMILY OF THE FULLY REMARK 900 REDUCED NATIVE CYTOCHROME C7 FROM DESULFUROMONAS ACETOXIDANS REMARK 900 RELATED ID: 1NEW RELATED DB: PDB REMARK 900 1NEW CONTAINS 18 SOLUTION STRUCTURES OF THE FULLY OXIDIZED NATIVE REMARK 900 CYTOCHROME C7 FROM DESULFUROMONAS ACETOXIDANS REMARK 900 RELATED ID: 2NEW RELATED DB: PDB REMARK 900 2NEW CONTAINS 17 SOLUTION STRUCTURES OF THE FULLY OXIDIZED NATIVE REMARK 900 CYTOCHROME C7 FROM DESULFUROMONAS ACETOXIDANS REMARK 900 RELATED ID: 1HH5 RELATED DB: PDB REMARK 900 1HH5 CONTAINS THE X-RAY STRUCTURE OF THE FULLY OXIDIZED NATIVE REMARK 900 CYTOCHROME C7 FROM DESULFUROMONAS ACETOXIDANS REMARK 900 RELATED ID: 1L3O RELATED DB: PDB REMARK 900 CONTAINS THE RELATED 35 STRUCTURE ENSEMBLE DBREF 1KWJ A 1 68 UNP P00137 CYC3_DESAC 1 68 SEQADV 1KWJ ALA A 9 UNP P00137 LYS 9 ENGINEERED MUTATION SEQADV 1KWJ ALA A 10 UNP P00137 LYS 10 ENGINEERED MUTATION SEQRES 1 A 68 ALA ASP VAL VAL THR TYR GLU ASN ALA ALA GLY ASN VAL SEQRES 2 A 68 THR PHE ASP HIS LYS ALA HIS ALA GLU LYS LEU GLY CYS SEQRES 3 A 68 ASP ALA CYS HIS GLU GLY THR PRO ALA LYS ILE ALA ILE SEQRES 4 A 68 ASP LYS LYS SER ALA HIS LYS ASP ALA CYS LYS THR CYS SEQRES 5 A 68 HIS LYS SER ASN ASN GLY PRO THR LYS CYS GLY GLY CYS SEQRES 6 A 68 HIS ILE LYS HET HEC A 130 75 HET HEC A 153 75 HET HEC A 166 75 HETNAM HEC HEME C FORMUL 2 HEC 3(C34 H34 FE N4 O4) HELIX 1 1 HIS A 17 GLY A 25 1 9 HELIX 2 2 CYS A 26 HIS A 30 5 5 HELIX 3 3 LYS A 42 ASP A 47 1 6 HELIX 4 4 CYS A 49 ASN A 56 1 8 HELIX 5 5 LYS A 61 HIS A 66 1 6 SHEET 1 A 2 VAL A 3 VAL A 4 0 SHEET 2 A 2 PHE A 15 ASP A 16 -1 O PHE A 15 N VAL A 4 LINK SG CYS A 26 CAB HEC A 130 1555 1555 1.81 LINK SG CYS A 29 CAC HEC A 130 1555 1555 1.82 LINK SG CYS A 49 CAB HEC A 153 1555 1555 1.82 LINK SG CYS A 52 CAC HEC A 153 1555 1555 1.81 LINK SG CYS A 62 CAB HEC A 166 1555 1555 1.82 LINK SG CYS A 65 CAC HEC A 166 1555 1555 1.82 LINK NE2 HIS A 17 FE HEC A 130 1555 1555 1.98 LINK NE2 HIS A 20 FE HEC A 153 1555 1555 1.99 LINK NE2 HIS A 30 FE HEC A 130 1555 1555 1.99 LINK NE2 HIS A 45 FE HEC A 166 1555 1555 1.98 LINK NE2 HIS A 53 FE HEC A 153 1555 1555 2.01 LINK NE2 HIS A 66 FE HEC A 166 1555 1555 1.99 SITE 1 AC1 14 ALA A 1 TYR A 6 HIS A 17 HIS A 20 SITE 2 AC1 14 ALA A 21 CYS A 26 CYS A 29 HIS A 30 SITE 3 AC1 14 PRO A 34 ALA A 35 LYS A 36 ILE A 37 SITE 4 AC1 14 ILE A 39 HEC A 153 SITE 1 AC2 9 VAL A 13 PHE A 15 HIS A 20 LYS A 23 SITE 2 AC2 9 ALA A 28 CYS A 49 CYS A 52 HIS A 53 SITE 3 AC2 9 HEC A 130 SITE 1 AC3 11 ASN A 8 ALA A 9 ALA A 10 ASP A 40 SITE 2 AC3 11 LYS A 41 ALA A 44 HIS A 45 CYS A 49 SITE 3 AC3 11 CYS A 62 CYS A 65 HIS 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
Complete list - 27 20 Bytes