Header list of 2fwl.pdb file
Complete list - r 25 2 Bytes
HEADER ELECTRON TRANSPORT/OXIDOREDUCTASE 02-FEB-06 2FWL TITLE THE CYTOCHROME C552/CUA COMPLEX FROM THERMUS THERMOPHILUS COMPND MOL_ID: 1; COMPND 2 MOLECULE: CYTOCHROME C-552; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: CYTOCHROME C552; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: CYTOCHROME C OXIDASE SUBUNIT II; COMPND 8 CHAIN: B; COMPND 9 SYNONYM: CYTOCHROME C OXIDASE SUBUNIT 2, CYTOCHROME C OXIDASE COMPND 10 POLYPEPTIDE II, BA3 OXIDASE SUBUNIT II, CUA DOMAIN; COMPND 11 EC: 1.9.3.1; COMPND 12 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS; SOURCE 3 ORGANISM_TAXID: 300852; SOURCE 4 STRAIN: HB8; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET-22B; SOURCE 10 MOL_ID: 2; SOURCE 11 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS; SOURCE 12 ORGANISM_TAXID: 300852; SOURCE 13 STRAIN: HB8; SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 15 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 16 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS; SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PET-3D KEYWDS DOCKING CALCULATIONS, REDOX PROTEIN COMPLEX, ELECTRON TRANSFER KEYWDS 2 PATHWAY, ELECTRON TRANSPORT-OXIDOREDUCTASE COMPLEX EXPDTA SOLUTION NMR NUMMDL 3 AUTHOR L.MURESANU,P.PRISTOVSEK,F.LOEHR,O.MANEG,M.D.MUKRASCH,H.RUETERJANS, AUTHOR 2 B.LUDWIG,C.LUECKE REVDAT 4 13-JUL-11 2FWL 1 VERSN REVDAT 3 24-FEB-09 2FWL 1 VERSN REVDAT 2 23-MAY-06 2FWL 1 JRNL REVDAT 1 28-MAR-06 2FWL 0 JRNL AUTH L.MURESANU,P.PRISTOVSEK,F.LOEHR,O.MANEG,M.D.MUKRASCH, JRNL AUTH 2 H.RUETERJANS,B.LUDWIG,C.LUECKE JRNL TITL THE ELECTRON TRANSFER COMPLEX BETWEEN CYTOCHROME C552 AND JRNL TITL 2 THE CUA DOMAIN OF THE THERMUS THERMOPHILUS BA3 OXIDASE - A JRNL TITL 3 COMBINED NMR AND COMPUTATIONAL APPROACH JRNL REF J.BIOL.CHEM. V. 281 14503 2006 JRNL REFN ISSN 0021-9258 JRNL PMID 16554303 JRNL DOI 10.1074/JBC.M601108200 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : HADDOCK 1.3 REMARK 3 AUTHORS : BONVIN REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 2FWL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-FEB-06. REMARK 100 THE RCSB ID CODE IS RCSB036398. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 6.0 REMARK 210 IONIC STRENGTH : 20MM PHOSPHATE BUFFER REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 0.5MM CYTOCHROME C552 U-15N, REMARK 210 20MM PHOSPHATE BUFFER, 2MM CUA REMARK 210 DOMAIN, 95% H2O, 5% D2O; 0.5MM REMARK 210 CUA DOMAIN U-15N, 20MM PHOSPHATE REMARK 210 BUFFER, 2MM CYTOCHROME C552, 95% REMARK 210 H2O, 5% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 15N_SEPARATED_TROSY REMARK 210 SPECTROMETER FIELD STRENGTH : 900 MHZ REMARK 210 SPECTROMETER MODEL : AVANCE REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : HADDOCK 1.3 REMARK 210 METHOD USED : DOCKING CALCULATIONS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 10 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 3 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 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: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B 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 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 MODELS 1-3 REMARK 465 RES C SSSEQI REMARK 465 MET A -1 REMARK 465 ALA A 0 REMARK 465 GLN A 1 REMARK 465 ALA A 2 REMARK 465 MET B 33 REMARK 465 ALA B 34 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 HE2 HIS A 32 O1A HEC A 132 1.58 REMARK 500 OE2 GLU A 124 HZ2 LYS A 127 1.59 REMARK 500 OE1 GLU A 59 HZ3 LYS A 64 1.59 REMARK 500 OE2 GLU B 51 HZ2 LYS B 106 1.59 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 GLN A 16 176.26 65.27 REMARK 500 1 ALA A 25 -53.69 -139.81 REMARK 500 1 HIS A 32 -32.99 -143.92 REMARK 500 1 ASN A 66 71.98 -156.38 REMARK 500 1 PHE A 72 45.83 -84.50 REMARK 500 1 GLN B 69 44.23 -88.07 REMARK 500 1 ALA B 87 103.31 -55.86 REMARK 500 1 ASP B 111 -97.71 -129.16 REMARK 500 1 PHE B 116 76.66 -110.66 REMARK 500 1 CYS B 153 89.67 170.52 REMARK 500 2 CYS A 14 -43.58 -130.43 REMARK 500 2 GLN A 16 -172.11 59.47 REMARK 500 2 ALA A 25 -48.43 -138.27 REMARK 500 2 ASN A 66 82.54 -156.84 REMARK 500 2 GLN B 60 -35.93 -130.90 REMARK 500 2 PHE B 86 -169.77 -75.01 REMARK 500 2 ALA B 87 93.75 -39.66 REMARK 500 2 ASP B 111 -111.76 -95.00 REMARK 500 2 CYS B 153 78.34 -176.55 REMARK 500 2 HIS B 157 -37.50 -131.71 REMARK 500 3 CYS A 14 -51.13 -153.56 REMARK 500 3 GLN A 16 -168.19 61.41 REMARK 500 3 GLN A 20 -80.16 -124.73 REMARK 500 3 PRO A 23 99.38 -57.77 REMARK 500 3 HIS A 32 -34.22 -146.06 REMARK 500 3 GLN A 57 82.80 -161.82 REMARK 500 3 LYS A 115 99.68 -68.25 REMARK 500 3 ALA B 87 102.94 -52.12 REMARK 500 3 ASP B 111 -113.98 -115.84 REMARK 500 3 CYS B 153 65.17 176.44 REMARK 500 3 HIS B 157 -59.30 -127.78 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 1 HEC A 132 FE REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS A 15 NE2 REMARK 620 2 HEC A 132 NA 91.1 REMARK 620 3 HEC A 132 NB 89.9 90.0 REMARK 620 4 HEC A 132 NC 89.7 179.2 89.9 REMARK 620 5 HEC A 132 ND 90.8 90.0 179.3 90.1 REMARK 620 6 MET A 69 SD 178.5 90.3 90.7 88.9 88.6 REMARK 620 N 1 2 3 4 5 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 1 CUA B 169 CU1 REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS B 149 SG REMARK 620 2 CUA B 169 CU2 57.5 REMARK 620 3 GLN B 151 O 94.4 111.4 REMARK 620 4 CYS B 153 SG 113.3 56.1 113.8 REMARK 620 5 HIS B 157 ND1 145.8 151.3 87.2 96.9 REMARK 620 N 1 2 3 4 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 1 CUA B 169 CU2 REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS B 114 ND1 REMARK 620 2 CUA B 169 CU1 150.7 REMARK 620 3 CYS B 149 SG 115.2 59.2 REMARK 620 4 CYS B 153 SG 117.6 63.1 122.0 REMARK 620 5 MET B 160 SD 86.7 122.5 104.2 101.0 REMARK 620 N 1 2 3 4 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 132 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CUA B 169 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1EHK RELATED DB: PDB REMARK 900 ATOM COORDINATES OF THE BA3 OXIDASE FROM THERMUS REMARK 900 THERMOPHILUS REMARK 900 RELATED ID: 1DT1 RELATED DB: PDB REMARK 900 ATOM COORDINATES OF THE CYTOCHROME C552 FROM THERMUS REMARK 900 THERMOPHILUS REMARK 900 RELATED ID: 6966 RELATED DB: BMRB REMARK 900 CHEMICAL SHIFT ASSIGNMENTS FOR THE REDUCED STATE OF CHAIN A REMARK 900 RELATED ID: 6967 RELATED DB: BMRB REMARK 900 CHEMICAL SHIFT ASSIGNMENTS FOR THE OXIDIZED STATE OF CHAIN A REMARK 900 RELATED ID: 5819 RELATED DB: BMRB REMARK 900 CHEMICAL SHIFT ASSIGNMENTS FOR THE REDUCED STATE OF CHAIN B REMARK 900 RELATED ID: 6965 RELATED DB: BMRB REMARK 900 CHEMICAL SHIFT ASSIGNMENTS FOR THE OXIDIZED STATE OF CHAIN B DBREF 2FWL A 1 131 UNP P04164 CY552_THETH 1 131 DBREF 2FWL B 34 168 UNP P98052 COX2_THETH 1 135 SEQADV 2FWL MET A -1 UNP P04164 CLONING ARTIFACT SEQADV 2FWL ALA A 0 UNP P04164 CLONING ARTIFACT SEQADV 2FWL MET B 33 UNP P98052 CLONING ARTIFACT SEQRES 1 A 133 MET ALA GLN ALA ASP GLY ALA LYS ILE TYR ALA GLN CYS SEQRES 2 A 133 ALA GLY CYS HIS GLN GLN ASN GLY GLN GLY ILE PRO GLY SEQRES 3 A 133 ALA PHE PRO PRO LEU ALA GLY HIS VAL ALA GLU ILE LEU SEQRES 4 A 133 ALA LYS GLU GLY GLY ARG GLU TYR LEU ILE LEU VAL LEU SEQRES 5 A 133 LEU TYR GLY LEU GLN GLY GLN ILE GLU VAL LYS GLY MET SEQRES 6 A 133 LYS TYR ASN GLY VAL MET SER SER PHE ALA GLN LEU LYS SEQRES 7 A 133 ASP GLU GLU ILE ALA ALA VAL LEU ASN HIS ILE ALA THR SEQRES 8 A 133 ALA TRP GLY ASP ALA LYS LYS VAL LYS GLY PHE LYS PRO SEQRES 9 A 133 PHE THR ALA GLU GLU VAL LYS LYS LEU ARG ALA LYS LYS SEQRES 10 A 133 LEU THR PRO GLN GLN VAL LEU ALA GLU ARG LYS LYS LEU SEQRES 11 A 133 GLY LEU LYS SEQRES 1 B 136 MET ALA TYR THR LEU ALA THR HIS THR ALA GLY VAL ILE SEQRES 2 B 136 PRO ALA GLY LYS LEU GLU ARG VAL ASP PRO THR THR VAL SEQRES 3 B 136 ARG GLN GLU GLY PRO TRP ALA ASP PRO ALA GLN ALA VAL SEQRES 4 B 136 VAL GLN THR GLY PRO ASN GLN TYR THR VAL TYR VAL LEU SEQRES 5 B 136 ALA PHE ALA PHE GLY TYR GLN PRO ASN PRO ILE GLU VAL SEQRES 6 B 136 PRO GLN GLY ALA GLU ILE VAL PHE LYS ILE THR SER PRO SEQRES 7 B 136 ASP VAL ILE HIS GLY PHE HIS VAL GLU GLY THR ASN ILE SEQRES 8 B 136 ASN VAL GLU VAL LEU PRO GLY GLU VAL SER THR VAL ARG SEQRES 9 B 136 TYR THR PHE LYS ARG PRO GLY GLU TYR ARG ILE ILE CYS SEQRES 10 B 136 ASN GLN TYR CYS GLY LEU GLY HIS GLN ASN MET PHE GLY SEQRES 11 B 136 THR ILE VAL VAL LYS GLU HET HEC A 132 75 HET CUA B 169 2 HETNAM HEC HEME C HETNAM CUA DINUCLEAR COPPER ION FORMUL 3 HEC C34 H34 FE N4 O4 FORMUL 4 CUA CU2 HELIX 1 1 ASP A 3 ALA A 12 1 10 HELIX 2 2 HIS A 32 ALA A 38 1 7 HELIX 3 3 GLY A 41 TYR A 52 1 12 HELIX 4 4 LYS A 76 TRP A 91 1 16 HELIX 5 5 GLY A 92 LYS A 96 5 5 HELIX 6 6 THR A 104 ALA A 113 1 10 HELIX 7 7 THR A 117 LEU A 128 1 12 HELIX 8 8 TYR B 35 ILE B 45 5 11 HELIX 9 9 GLY B 156 ASN B 159 5 4 SHEET 1 A 2 GLU A 59 VAL A 60 0 SHEET 2 A 2 MET A 63 LYS A 64 -1 O MET A 63 N VAL A 60 SHEET 1 B 3 VAL B 71 GLY B 75 0 SHEET 2 B 3 GLN B 78 PHE B 86 -1 O THR B 80 N VAL B 72 SHEET 3 B 3 GLY B 89 GLN B 91 -1 O GLN B 91 N LEU B 84 SHEET 1 C 4 VAL B 71 GLY B 75 0 SHEET 2 C 4 GLN B 78 PHE B 86 -1 O THR B 80 N VAL B 72 SHEET 3 C 4 GLU B 102 THR B 108 1 O THR B 108 N ALA B 85 SHEET 4 C 4 SER B 133 THR B 138 -1 O TYR B 137 N ILE B 103 SHEET 1 D 5 ILE B 95 PRO B 98 0 SHEET 2 D 5 PHE B 161 LYS B 167 1 O THR B 163 N ILE B 95 SHEET 3 D 5 GLY B 143 ILE B 148 -1 N TYR B 145 O ILE B 164 SHEET 4 D 5 HIS B 114 VAL B 118 -1 N HIS B 117 O ILE B 148 SHEET 5 D 5 ASN B 124 VAL B 127 -1 O VAL B 125 N PHE B 116 LINK FE HEC A 132 NE2 HIS A 15 1555 1555 2.00 LINK FE HEC A 132 SD MET A 69 1555 1555 2.30 LINK CAB HEC A 132 SG CYS A 11 1555 1555 1.82 LINK CAC HEC A 132 SG CYS A 14 1555 1555 1.82 LINK CU1 CUA B 169 SG CYS B 149 1555 1555 2.34 LINK CU1 CUA B 169 O GLN B 151 1555 1555 1.78 LINK CU1 CUA B 169 SG CYS B 153 1555 1555 2.49 LINK CU1 CUA B 169 ND1 HIS B 157 1555 1555 2.13 LINK CU2 CUA B 169 ND1 HIS B 114 1555 1555 2.11 LINK CU2 CUA B 169 SG CYS B 149 1555 1555 2.30 LINK CU2 CUA B 169 SG CYS B 153 1555 1555 2.32 LINK CU2 CUA B 169 SD MET B 160 1555 1555 2.51 CISPEP 1 GLN B 91 PRO B 92 1 -0.20 CISPEP 2 ASN B 93 PRO B 94 1 -1.33 CISPEP 3 GLN B 91 PRO B 92 2 -0.15 CISPEP 4 ASN B 93 PRO B 94 2 -0.36 CISPEP 5 GLN B 91 PRO B 92 3 -0.36 CISPEP 6 ASN B 93 PRO B 94 3 0.18 SITE 1 AC1 19 GLN A 10 CYS A 11 CYS A 14 HIS A 15 SITE 2 AC1 19 ALA A 25 PHE A 26 PRO A 27 HIS A 32 SITE 3 AC1 19 TYR A 45 LEU A 54 GLN A 55 GLY A 56 SITE 4 AC1 19 GLY A 67 VAL A 68 MET A 69 SER A 70 SITE 5 AC1 19 PHE A 72 ARG A 125 ALA B 87 SITE 1 AC2 7 HIS B 114 CYS B 149 GLN B 151 TYR B 152 SITE 2 AC2 7 CYS B 153 HIS B 157 MET B 160 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 25 2 Bytes