Header list of 1lm2.pdb file
Complete list - b 23 2 Bytes
HEADER ELECTRON TRANSPORT 30-APR-02 1LM2 TITLE NMR STRUCTURAL CHARACTERIZATION OF THE REDUCTION OF CHROMIUM(VI) TO TITLE 2 CHROMIUM(III) BY CYTOCHROME C7 COMPND MOL_ID: 1; COMPND 2 MOLECULE: CYTOCHROME C7; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: CYTOCHROME C3, CYTOCHROME C551.5 SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: DESULFUROMONAS ACETOXIDANS; SOURCE 3 ORGANISM_TAXID: 891 KEYWDS CHROMIUM, CYTOCHROME C7, ELECTRON TRANSPORT EXPDTA SOLUTION NMR NUMMDL 35 AUTHOR M.ASSFALG,I.BERTINI,M.BRUSCHI,C.MICHEL,P.TURANO REVDAT 4 23-FEB-22 1LM2 1 REMARK LINK REVDAT 3 24-FEB-09 1LM2 1 VERSN REVDAT 2 01-APR-03 1LM2 1 JRNL REVDAT 1 31-JUL-02 1LM2 0 JRNL AUTH M.ASSFALG,I.BERTINI,M.BRUSCHI,C.MICHEL,P.TURANO JRNL TITL THE METAL REDUCTASE ACTIVITY OF SOME MULTIHEME CYTOCHROMES JRNL TITL 2 C: NMR STRUCTURAL CHARACTERIZATION OF THE REDUCTION OF JRNL TITL 3 CHROMIUM(VI) TO CHROMIUM(III) BY CYTOCHROME C(7). JRNL REF PROC.NATL.ACAD.SCI.USA V. 99 9750 2002 JRNL REFN ISSN 0027-8424 JRNL PMID 12119407 JRNL DOI 10.1073/PNAS.152290999 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : DYANA 1.5, DYANA 1.5 REMARK 3 AUTHORS : GUENTERT (DYANA), GUENTERT (DYANA) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1LM2 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-MAY-02. REMARK 100 THE DEPOSITION ID IS D_1000016073. 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 BUFFER REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : 2 MM CYTOCHROME C7-CHROMIUM(III) REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 700 MHZ REMARK 210 SPECTROMETER MODEL : DRX 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 REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 500 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 35 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH BEST TARGET REMARK 210 FUNCTION REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: THE PROTEIN SOLUTION WAS TITRATED BY ADDITION OF REMARK 210 INCREASING AMOUNTS OF THE (CRO4)2- SOLUTION DIRECTLY IN THE NMR REMARK 210 TUBE. THE (CRO4)2- SOLUTION WAS KEPT UNDER ARGON ATMOSPHERE TO REMARK 210 AVOID THE PRESENCE OF OXYGEN IN THE NMR TUBE. 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 CYS A 26 H CYS A 29 1.48 REMARK 500 O SER A 43 H LYS A 46 1.51 REMARK 500 SG CYS A 29 HAC HEC A 98 1.54 REMARK 500 SG CYS A 62 HAB HEC A 158 1.54 REMARK 500 O ASP A 2 H HIS A 17 1.56 REMARK 500 SG CYS A 29 CAC HEC A 98 2.12 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 2 -46.69 -146.25 REMARK 500 1 THR A 14 98.94 -58.29 REMARK 500 1 LEU A 24 -101.80 -60.72 REMARK 500 1 CYS A 26 -75.77 64.36 REMARK 500 1 ASP A 27 -31.48 -39.37 REMARK 500 1 THR A 33 104.72 67.40 REMARK 500 1 ALA A 35 -55.46 173.12 REMARK 500 1 ALA A 38 87.72 39.73 REMARK 500 1 ASP A 40 -66.05 -172.17 REMARK 500 1 LYS A 41 80.64 -175.50 REMARK 500 1 LYS A 42 -49.96 172.26 REMARK 500 1 LYS A 46 -162.58 -113.12 REMARK 500 1 CYS A 49 -64.99 -102.44 REMARK 500 1 LYS A 50 95.79 -56.38 REMARK 500 1 THR A 51 -58.32 171.51 REMARK 500 1 CYS A 52 62.41 -102.74 REMARK 500 1 HIS A 53 -46.11 -148.95 REMARK 500 1 LYS A 54 80.74 -61.85 REMARK 500 1 SER A 55 -50.29 169.69 REMARK 500 1 ASN A 57 -66.04 78.08 REMARK 500 1 LYS A 61 -158.99 -92.91 REMARK 500 1 CYS A 65 -71.05 -87.35 REMARK 500 1 HIS A 66 89.97 -54.58 REMARK 500 1 ILE A 67 108.11 -44.86 REMARK 500 2 ASP A 2 -28.75 158.12 REMARK 500 2 VAL A 3 129.45 -174.61 REMARK 500 2 LYS A 10 -76.04 -40.24 REMARK 500 2 GLU A 22 -33.13 -37.03 REMARK 500 2 LYS A 23 -60.39 -109.52 REMARK 500 2 LEU A 24 -76.97 -41.54 REMARK 500 2 CYS A 26 -68.08 74.19 REMARK 500 2 THR A 33 104.42 67.63 REMARK 500 2 ALA A 35 -50.15 -178.35 REMARK 500 2 LYS A 36 -172.17 -176.64 REMARK 500 2 ASP A 40 -64.10 -166.21 REMARK 500 2 LYS A 41 -117.34 -143.78 REMARK 500 2 LYS A 46 -158.46 -107.91 REMARK 500 2 CYS A 49 -73.08 -107.47 REMARK 500 2 LYS A 50 98.96 -47.24 REMARK 500 2 THR A 51 -72.81 -177.44 REMARK 500 2 HIS A 53 -48.51 -159.36 REMARK 500 2 SER A 55 -62.24 -171.55 REMARK 500 2 ASN A 56 -60.70 -97.60 REMARK 500 2 ASN A 57 -84.38 -40.81 REMARK 500 2 LYS A 61 -162.97 -110.43 REMARK 500 3 GLU A 7 42.45 -148.26 REMARK 500 3 ASN A 8 177.95 -59.91 REMARK 500 3 THR A 14 71.39 -102.75 REMARK 500 3 PHE A 15 164.45 -44.93 REMARK 500 3 ALA A 21 -30.43 -39.89 REMARK 500 REMARK 500 THIS ENTRY HAS 805 RAMACHANDRAN OUTLIERS. 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 98 FE REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS A 17 NE2 REMARK 620 2 HEC A 98 NA 92.7 REMARK 620 3 HEC A 98 NB 78.3 91.1 REMARK 620 4 HEC A 98 NC 89.2 177.1 91.5 REMARK 620 5 HEC A 98 ND 103.4 87.9 178.1 89.5 REMARK 620 6 HIS A 30 NE2 162.5 83.7 84.7 95.1 93.6 REMARK 620 N 1 2 3 4 5 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 HEC A 128 FE REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS A 20 NE2 REMARK 620 2 HEC A 128 NA 93.6 REMARK 620 3 HEC A 128 NB 100.6 91.1 REMARK 620 4 HEC A 128 NC 87.3 177.1 91.5 REMARK 620 5 HEC A 128 ND 81.1 87.9 178.0 89.5 REMARK 620 6 HIS A 53 NE2 169.8 96.5 80.6 82.6 97.8 REMARK 620 N 1 2 3 4 5 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 HEC A 158 FE REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS A 45 NE2 REMARK 620 2 HEC A 158 NA 100.2 REMARK 620 3 HEC A 158 NB 91.7 91.1 REMARK 620 4 HEC A 158 NC 81.1 177.0 91.5 REMARK 620 5 HEC A 158 ND 90.1 87.9 178.1 89.5 REMARK 620 6 HIS A 66 NE2 170.5 81.1 78.9 98.0 99.4 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 HEC A 98 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC A 128 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC A 158 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1NEW RELATED DB: PDB REMARK 900 CONTAINS THE 18 OF 35 NMR STRUCTURES OF THE FULLY OXIDIZED REMARK 900 CYTOCHROME C7 FROM D. ACETOXIDANS REMARK 900 RELATED ID: 2NEW RELATED DB: PDB REMARK 900 CONTAINS THE 17 OF 35 NMR STRUCTURES OF THE FULLY OXIDIZED REMARK 900 CYTOCHROME C7 FROM D. ACETOXIDANS REMARK 900 RELATED ID: 1EHJ RELATED DB: PDB REMARK 900 CONTAINS THE ENERGY MINIMIZED NMR AVERAGE STRUCTURE OF THE FULLY REMARK 900 REDUCED CYTOCHROME C7 FROM D. ACETOXIDANS REMARK 900 RELATED ID: 1HH5 RELATED DB: PDB REMARK 900 CONTAINS THE X-RAY STRUCTURE OF CYTOCHROME C7 FROM D. ACETOXIDANS DBREF 1LM2 A 1 68 UNP P00137 CYC3_DESAC 1 68 SEQRES 1 A 68 ALA ASP VAL VAL THR TYR GLU ASN LYS LYS 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 CR A 188 1 HET HEC A 98 75 HET HEC A 128 75 HET HEC A 158 75 HETNAM CR CHROMIUM ION HETNAM HEC HEME C FORMUL 2 CR CR 3+ FORMUL 3 HEC 3(C34 H34 FE N4 O4) HELIX 1 1 HIS A 17 GLU A 22 1 6 LINK SG CYS A 26 CAB HEC A 98 1555 1555 1.93 LINK SG CYS A 49 CAB HEC A 128 1555 1555 1.97 LINK SG CYS A 52 CAC HEC A 128 1555 1555 1.84 LINK SG CYS A 62 CAB HEC A 158 1555 1555 2.08 LINK SG CYS A 65 CAC HEC A 158 1555 1555 1.94 LINK NE2 HIS A 17 FE HEC A 98 1555 1555 2.10 LINK NE2 HIS A 20 FE HEC A 128 1555 1555 2.22 LINK NE2 HIS A 30 FE HEC A 98 1555 1555 1.95 LINK NE2 HIS A 45 FE HEC A 158 1555 1555 2.20 LINK NE2 HIS A 53 FE HEC A 128 1555 1555 2.20 LINK NE2 HIS A 66 FE HEC A 158 1555 1555 2.12 SITE 1 AC1 11 TYR A 6 HIS A 17 LEU A 24 CYS A 26 SITE 2 AC1 11 CYS A 29 HIS A 30 PRO A 34 ALA A 35 SITE 3 AC1 11 ILE A 37 ILE A 39 HEC A 128 SITE 1 AC2 14 VAL A 13 PHE A 15 ALA A 19 HIS A 20 SITE 2 AC2 14 LEU A 24 ALA A 28 CYS A 29 ALA A 48 SITE 3 AC2 14 CYS A 49 CYS A 52 HIS A 53 ASN A 57 SITE 4 AC2 14 CYS A 65 HEC A 98 SITE 1 AC3 14 TYR A 6 ASN A 8 LYS A 10 VAL A 13 SITE 2 AC3 14 PHE A 15 ILE A 39 ASP A 40 ALA A 44 SITE 3 AC3 14 HIS A 45 THR A 60 LYS A 61 CYS A 62 SITE 4 AC3 14 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 MODEL 1
Complete list - b 23 2 Bytes