Header list of 2ai5.pdb file
Complete list - r 9 2 Bytes
HEADER ELECTRON TRANSPORT 29-JUL-05 2AI5 TITLE SOLUTION STRUCTURE OF CYTOCHROME C552, DETERMINED BY DISTRIBUTED TITLE 2 COMPUTING IMPLEMENTATION FOR NMR DATA COMPND MOL_ID: 1; COMPND 2 MOLECULE: CYTOCHROME C-552; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: CYTOCHROME C552 SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HYDROGENOBACTER THERMOPHILUS; SOURCE 3 ORGANISM_TAXID: 940; SOURCE 4 STRAIN: TK-6 KEYWDS CYTOCHROME C, ELECTRON TRANSPORT, PORPHYRIN, FERROUS IRON EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR S.NAKAMURA,S.I.ICHIKI,H.TAKASHIMA,S.UCHIYAMA,J.HASEGAWA,Y.KOBAYASHI, AUTHOR 2 Y.SAMBONGI,T.OHKUBO REVDAT 3 09-MAR-22 2AI5 1 REMARK LINK REVDAT 2 24-FEB-09 2AI5 1 VERSN REVDAT 1 23-MAY-06 2AI5 0 JRNL AUTH S.NAKAMURA,S.I.ICHIKI,H.TAKASHIMA,S.UCHIYAMA,J.HASEGAWA, JRNL AUTH 2 Y.KOBAYASHI,Y.SAMBONGI,T.OHKUBO JRNL TITL STRUCTURE OF CYTOCHROME C552 FROM A MODERATE THERMOPHILIC JRNL TITL 2 BACTERIUM, HYDROGENOPHILUS THERMOLUTEOLUS: COMPARATIVE STUDY JRNL TITL 3 ON THE THERMOSTABILITY OF CYTOCHROME C JRNL REF BIOCHEMISTRY V. 45 6115 2006 JRNL REFN ISSN 0006-2960 JRNL PMID 16681384 JRNL DOI 10.1021/BI0520131 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR XPLOR-NIH V2.0.6, X-PLOR XPLOR-NIH V2.0.6 REMARK 3 AUTHORS : SCHWIETERS, C. D. (X-PLOR), SCHWIETERS, C. D. (X REMARK 3 -PLOR) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: DISTRIBUTED COMPUTING REMARK 4 REMARK 4 2AI5 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 02-AUG-05. REMARK 100 THE DEPOSITION ID IS D_1000033923. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 4.8 REMARK 210 IONIC STRENGTH : 120MM ACETATE BUFFER REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : 2MM CYTOCHROME C-552 REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ REMARK 210 SPECTROMETER MODEL : DMX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NULL REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 4000 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST REMARK 210 ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: THE 1H-NMR DATA WERE SUBJECTED TO THE STRUCTURE REMARK 210 DETERMINATION USING DISTRIBUTED COMPUTING IMPLEMENTATIONS. 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: 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 GLU A 2 -67.53 68.20 REMARK 500 1 CYS A 13 -37.05 -136.44 REMARK 500 1 ASP A 15 125.47 176.55 REMARK 500 1 LYS A 19 85.39 -55.51 REMARK 500 1 LYS A 20 -143.47 -96.63 REMARK 500 1 LEU A 42 -74.66 -43.21 REMARK 500 1 SER A 51 -170.30 169.92 REMARK 500 1 VAL A 57 102.66 -42.19 REMARK 500 1 PRO A 58 87.50 -60.80 REMARK 500 1 ASN A 63 72.75 -103.81 REMARK 500 2 CYS A 13 -34.15 -132.27 REMARK 500 2 ASP A 15 124.96 169.39 REMARK 500 2 ALA A 18 45.75 -147.73 REMARK 500 2 LYS A 19 94.22 -42.40 REMARK 500 2 LYS A 20 -89.71 -89.73 REMARK 500 2 LEU A 42 -73.98 -43.08 REMARK 500 2 SER A 51 -175.82 169.76 REMARK 500 2 SER A 56 54.40 -110.09 REMARK 500 2 PRO A 58 88.74 -60.51 REMARK 500 2 ASN A 63 62.10 -104.82 REMARK 500 3 CYS A 13 -36.03 -135.95 REMARK 500 3 ASP A 15 124.08 172.73 REMARK 500 3 LYS A 19 78.36 -60.31 REMARK 500 3 LYS A 20 -141.68 -88.42 REMARK 500 3 ASP A 37 34.26 -88.41 REMARK 500 3 LEU A 42 -73.66 -43.01 REMARK 500 3 SER A 51 -170.09 169.75 REMARK 500 3 PRO A 58 87.14 -60.86 REMARK 500 3 ASN A 63 57.05 -104.40 REMARK 500 4 ASP A 15 123.28 169.06 REMARK 500 4 ALA A 18 45.50 -148.30 REMARK 500 4 LYS A 19 93.64 -43.87 REMARK 500 4 LYS A 20 -89.87 -91.60 REMARK 500 4 LEU A 42 -73.99 -43.24 REMARK 500 4 SER A 51 177.05 169.69 REMARK 500 4 SER A 56 57.39 -108.05 REMARK 500 4 PRO A 58 78.08 -60.61 REMARK 500 4 ASN A 63 69.10 -104.09 REMARK 500 5 GLU A 2 -55.84 -175.69 REMARK 500 5 ASP A 15 122.88 170.66 REMARK 500 5 LYS A 19 86.57 -55.24 REMARK 500 5 LYS A 20 -147.48 -95.01 REMARK 500 5 LEU A 42 -73.90 -43.52 REMARK 500 5 SER A 51 -170.87 169.92 REMARK 500 5 SER A 56 65.34 -107.89 REMARK 500 5 PRO A 58 87.55 -60.59 REMARK 500 5 ASN A 63 64.08 -104.83 REMARK 500 6 GLN A 3 -84.22 -51.09 REMARK 500 6 CYS A 13 -36.82 -135.76 REMARK 500 6 HIS A 14 -178.84 -69.47 REMARK 500 REMARK 500 THIS ENTRY HAS 189 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 81 FE REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS A 14 NE2 REMARK 620 2 HEC A 81 NA 88.1 REMARK 620 3 HEC A 81 NB 89.4 90.1 REMARK 620 4 HEC A 81 NC 91.0 179.0 90.0 REMARK 620 5 HEC A 81 ND 89.6 90.3 179.0 89.6 REMARK 620 6 MET A 59 SD 174.5 86.4 90.6 94.6 90.4 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 81 DBREF 2AI5 A 1 80 UNP P15452 CY552_HYDTH 19 98 SEQRES 1 A 80 ASN GLU GLN LEU ALA LYS GLN LYS GLY CYS MET ALA CYS SEQRES 2 A 80 HIS ASP LEU LYS ALA LYS LYS VAL GLY PRO ALA TYR ALA SEQRES 3 A 80 ASP VAL ALA LYS LYS TYR ALA GLY ARG LYS ASP ALA VAL SEQRES 4 A 80 ASP TYR LEU ALA GLY LYS ILE LYS LYS GLY GLY SER GLY SEQRES 5 A 80 VAL TRP GLY SER VAL PRO MET PRO PRO GLN ASN VAL THR SEQRES 6 A 80 ASP ALA GLU ALA LYS GLN LEU ALA GLN TRP ILE LEU SER SEQRES 7 A 80 ILE LYS HET HEC A 81 75 HETNAM HEC HEME C FORMUL 2 HEC C34 H34 FE N4 O4 HELIX 1 1 GLU A 2 GLY A 9 1 8 HELIX 2 2 CYS A 10 CYS A 13 5 4 HELIX 3 3 ALA A 24 GLY A 34 1 11 HELIX 4 4 ASP A 37 LYS A 47 1 11 HELIX 5 5 THR A 65 ILE A 79 1 15 LINK SG CYS A 10 CAB HEC A 81 1555 1555 1.81 LINK SG CYS A 13 CAC HEC A 81 1555 1555 1.81 LINK NE2 HIS A 14 FE HEC A 81 1555 1555 2.20 LINK SD MET A 59 FE HEC A 81 1555 1555 2.13 SITE 1 AC1 21 LYS A 8 CYS A 10 ALA A 12 CYS A 13 SITE 2 AC1 21 HIS A 14 VAL A 21 TYR A 25 TYR A 41 SITE 3 AC1 21 LEU A 42 LYS A 45 ILE A 46 SER A 51 SITE 4 AC1 21 GLY A 52 VAL A 53 TRP A 54 GLY A 55 SITE 5 AC1 21 VAL A 57 MET A 59 PRO A 60 GLN A 62 SITE 6 AC1 21 LEU A 72 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