Header list of 1yjj.pdb file
Complete list - r 2 2 Bytes
HEADER ELECTRON TRANSPORT 14-JAN-05 1YJJ TITLE RDC-REFINED SOLUTION NMR STRUCTURE OF OXIDIZED PUTIDAREDOXIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: PUTIDAREDOXIN; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: PDX; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS PUTIDA; SOURCE 3 ORGANISM_TAXID: 303; SOURCE 4 GENE: CAMB; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: NCM533; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PUC19; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PKM536 KEYWDS FERREDOXIN, [2FE-2S], REDOX, IRON-SULFUR, ELECTRON TRANSFER, KEYWDS 2 CYTOCHROME P450CAM, ELECTRON TRANSPORT EXPDTA SOLUTION NMR NUMMDL 15 AUTHOR N.U.JAIN,E.TJIOE,A.SAVIDOR,J.BOULIE REVDAT 3 02-MAR-22 1YJJ 1 REMARK REVDAT 2 24-FEB-09 1YJJ 1 VERSN REVDAT 1 28-JUN-05 1YJJ 0 JRNL AUTH N.U.JAIN,E.TJIOE,A.SAVIDOR,J.BOULIE JRNL TITL REDOX-DEPENDENT STRUCTURAL DIFFERENCES IN PUTIDAREDOXIN JRNL TITL 2 DERIVED FROM HOMOLOGOUS STRUCTURE REFINEMENT VIA RESIDUAL JRNL TITL 3 DIPOLAR COUPLINGS. JRNL REF BIOCHEMISTRY V. 44 9067 2005 JRNL REFN ISSN 0006-2960 JRNL PMID 15966730 JRNL DOI 10.1021/BI050152C REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH T.C.POCHAPSKY,N.U.JAIN,M.KUTI,T.A.LYONS,J.HEYMONT REMARK 1 TITL A REFINED MODEL FOR THE SOLUTION STRUCTURE OF OXIDIZED REMARK 1 TITL 2 PUTIDAREDOXIN REMARK 1 REF BIOCHEMISTRY V. 38 4681 1999 REMARK 1 REFN ISSN 0006-2960 REMARK 1 PMID 10200155 REMARK 1 DOI 10.1021/BI983030B REMARK 1 REFERENCE 2 REMARK 1 AUTH A.MULLER,J.J.MULLER,Y.A.MULLER,H.UHLMANN,R.BERNHARDT, REMARK 1 AUTH 2 U.HEINEMANN REMARK 1 TITL NEW ASPECTS OF ELECTRON TRANSFER REVEALED BY THE CRYSTAL REMARK 1 TITL 2 STRUCTURE OF A TRUNCATED BOVINE ADRENODOXIN, ADX(4-108) REMARK 1 REF STRUCTURE V. 6 269 1998 REMARK 1 REFN ISSN 0969-2126 REMARK 1 PMID 9551550 REMARK 1 DOI 10.1016/S0969-2126(98)00031-8 REMARK 1 REFERENCE 3 REMARK 1 AUTH T.C.POCHAPSKY,X.M.YE,G.RATNASWAMY,T.A.LYONS REMARK 1 TITL AN NMR-DERIVED MODEL FOR THE SOLUTION STRUCTURE OF OXIDIZED REMARK 1 TITL 2 PUTIDAREDOXIN, A 2FE-2S FERREDOXIN FROM PSEUDOMONAS REMARK 1 REF BIOCHEMISTRY V. 33 6424 1994 REMARK 1 REFN ISSN 0006-2960 REMARK 1 PMID 8204575 REMARK 1 DOI 10.1021/BI00187A006 REMARK 1 REFERENCE 4 REMARK 1 AUTH I.F.SEVRIOUKOVA,C.GARCIA,H.LI,B.BHASKAR,T.L.POULOS REMARK 1 TITL CRYSTAL STRUCTURE OF PUTIDAREDOXIN, THE [2FE-2S] COMPONENT REMARK 1 TITL 2 OF THE P450CAM MONOOXYGENASE SYSTEM FROM PSEUDOMONAS PUTIDA REMARK 1 REF J.MOL.BIOL. V. 333 377 2003 REMARK 1 REFN ISSN 0022-2836 REMARK 1 PMID 14529624 REMARK 1 DOI 10.1016/J.JMB.2003.08.028 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XPLOR-NIH 2.9.6 REMARK 3 AUTHORS : SCHWIETERS, KUSZEWSKI, TJANDRA, CLORE REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON 1239 NOE REMARK 3 RESTRIANTS, 160 DIHEDRAL ANGLE RESTRAINTS AND 155 RDC RESTRAINTS, REMARK 3 28 PARAMAGNETIC DISTANCE RESTRAINTS FROM RELAXATION REMARK 3 MEASUREMENTS AND 18 DISTANCE RESTRIANTS FROM HYDROGEN BONDS REMARK 4 REMARK 4 1YJJ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-JAN-05. REMARK 100 THE DEPOSITION ID IS D_1000031584. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 7.4 REMARK 210 IONIC STRENGTH : 50 MM KCL REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1 MM OXIDIZED PUTIDAREDOXIN 15N; REMARK 210 50 MM TRIS-CL BUFFER, 50 MM KCL, REMARK 210 PH 7.4 REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 15N-COUPLED 2D 15N-1H HSQC; 7.5% REMARK 210 BICELLE (DMPC:DHPC-2.9:1); 15N- REMARK 210 COUPLED 2D 15N-1H HSQC; 10 MG/ML REMARK 210 PHAGE REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : INOVA REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NULL REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 50 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST REMARK 210 ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 2 REMARK 210 REMARK 210 REMARK: THE STRUCTURES WERE REFINED AGAINST 15N-1H RDC RESTRAINTS REMARK 210 USING PREVIOUSLY PUBLISHED NOE AND DIHEDRAL ANGLE RESTRAINTS FOR REMARK 210 PDX. THE RESTRAINTS FOR THE METAL BINDING LOOP (RESIDUES 36-48, REMARK 210 85-86) WERE MODELED FROM BOVINE ADRENODOXIN CRYSTAL STRUCTURE. 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 TYR A 33 H ILE A 35 1.19 REMARK 500 H ALA A 63 HH12 ARG A 83 1.35 REMARK 500 HH TYR A 51 O GLU A 77 1.46 REMARK 500 O TYR A 51 H ASP A 100 1.49 REMARK 500 H TYR A 51 O ASP A 100 1.54 REMARK 500 O TYR A 33 N ILE A 35 2.15 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 34 40.65 -54.28 REMARK 500 1 SER A 44 18.45 -146.73 REMARK 500 1 CYS A 48 36.55 -87.24 REMARK 500 1 GLU A 54 -1.85 -47.48 REMARK 500 1 ALA A 62 127.78 -36.06 REMARK 500 2 ASP A 34 -99.35 -59.24 REMARK 500 2 ILE A 35 85.40 31.52 REMARK 500 2 VAL A 36 98.58 52.90 REMARK 500 2 ASP A 38 -72.61 -68.93 REMARK 500 2 CYS A 48 36.97 -82.82 REMARK 500 2 GLU A 54 0.93 -47.99 REMARK 500 2 ALA A 62 130.60 -37.23 REMARK 500 3 ILE A 32 -52.46 -123.51 REMARK 500 3 ASP A 34 -98.72 -56.84 REMARK 500 3 VAL A 36 104.22 61.58 REMARK 500 3 ASP A 38 -73.87 -70.94 REMARK 500 3 SER A 42 11.49 -143.84 REMARK 500 3 SER A 44 21.28 -148.55 REMARK 500 3 CYS A 48 39.36 -90.99 REMARK 500 3 GLU A 54 -1.37 -47.20 REMARK 500 3 CYS A 85 2.13 -61.54 REMARK 500 4 ASP A 34 45.31 -49.65 REMARK 500 4 ASP A 38 -71.87 -68.62 REMARK 500 4 SER A 44 19.31 -146.95 REMARK 500 4 CYS A 48 37.64 -84.45 REMARK 500 4 GLU A 54 -4.72 -47.05 REMARK 500 5 ASP A 34 53.17 -49.10 REMARK 500 5 ILE A 35 -83.49 -104.58 REMARK 500 5 VAL A 36 129.85 -172.38 REMARK 500 5 ASP A 38 -72.22 -66.13 REMARK 500 5 CYS A 48 37.57 -78.64 REMARK 500 5 GLU A 54 -2.34 -48.50 REMARK 500 5 ALA A 62 129.66 -39.77 REMARK 500 6 ASP A 34 -100.32 -57.71 REMARK 500 6 VAL A 36 107.25 63.19 REMARK 500 6 ASP A 38 -72.38 -69.03 REMARK 500 6 SER A 44 18.92 -147.04 REMARK 500 6 CYS A 48 36.86 -87.43 REMARK 500 6 GLU A 54 -1.37 -47.73 REMARK 500 6 ALA A 62 139.15 -38.58 REMARK 500 6 GLN A 105 -33.08 -130.97 REMARK 500 7 ASP A 34 -98.52 -55.04 REMARK 500 7 ILE A 35 88.35 33.11 REMARK 500 7 VAL A 36 91.67 28.46 REMARK 500 7 ASP A 38 -72.16 -68.27 REMARK 500 7 SER A 44 18.72 -146.87 REMARK 500 7 CYS A 48 36.87 -82.69 REMARK 500 7 GLU A 54 2.07 -48.58 REMARK 500 8 TYR A 33 13.69 -68.23 REMARK 500 8 ASP A 34 44.56 -51.33 REMARK 500 REMARK 500 THIS ENTRY HAS 99 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 FES A 107 FE1 REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 39 SG REMARK 620 2 FES A 107 S1 108.8 REMARK 620 3 FES A 107 S2 104.3 103.8 REMARK 620 4 CYS A 45 SG 127.5 100.0 110.4 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 FES A 107 FE2 REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 48 SG REMARK 620 2 FES A 107 S1 107.7 REMARK 620 3 FES A 107 S2 105.7 104.0 REMARK 620 4 CYS A 86 SG 119.8 106.4 112.1 REMARK 620 N 1 2 3 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES A 107 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1PDX RELATED DB: PDB REMARK 900 RELATED ID: 4154 RELATED DB: BMRB REMARK 900 RELATED ID: 1YJI RELATED DB: PDB DBREF 1YJJ A 1 106 UNP P00259 PUTX_PSEPU 1 106 SEQRES 1 A 106 SER LYS VAL VAL TYR VAL SER HIS ASP GLY THR ARG ARG SEQRES 2 A 106 GLU LEU ASP VAL ALA ASP GLY VAL SER LEU MET GLN ALA SEQRES 3 A 106 ALA VAL SER ASN GLY ILE TYR ASP ILE VAL GLY ASP CYS SEQRES 4 A 106 GLY GLY SER ALA SER CYS ALA THR CYS HIS VAL TYR VAL SEQRES 5 A 106 ASN GLU ALA PHE THR ASP LYS VAL PRO ALA ALA ASN GLU SEQRES 6 A 106 ARG GLU ILE GLY MET LEU GLU CYS VAL THR ALA GLU LEU SEQRES 7 A 106 LYS PRO ASN SER ARG LEU CYS CYS GLN ILE ILE MET THR SEQRES 8 A 106 PRO GLU LEU ASP GLY ILE VAL VAL ASP VAL PRO ASP ARG SEQRES 9 A 106 GLN TRP HET FES A 107 4 HETNAM FES FE2/S2 (INORGANIC) CLUSTER FORMUL 2 FES FE2 S2 HELIX 1 1 SER A 22 ASN A 30 1 9 HELIX 2 2 ASN A 53 ASP A 58 1 6 HELIX 3 3 ASN A 64 GLU A 72 1 9 HELIX 4 4 THR A 91 ASP A 95 5 5 SHEET 1 A 5 ARG A 12 ASP A 16 0 SHEET 2 A 5 LYS A 2 VAL A 6 -1 N TYR A 5 O ARG A 13 SHEET 3 A 5 ILE A 97 ASP A 100 1 O VAL A 99 N VAL A 6 SHEET 4 A 5 VAL A 50 VAL A 52 -1 N TYR A 51 O ASP A 100 SHEET 5 A 5 SER A 82 ARG A 83 -1 O ARG A 83 N VAL A 50 LINK SG CYS A 39 FE1 FES A 107 1555 1555 2.20 LINK SG CYS A 45 FE1 FES A 107 1555 1555 2.20 LINK SG CYS A 48 FE2 FES A 107 1555 1555 2.20 LINK SG CYS A 86 FE2 FES A 107 1555 1555 2.19 SITE 1 AC1 8 TYR A 33 CYS A 39 ALA A 43 SER A 44 SITE 2 AC1 8 CYS A 45 CYS A 48 MET A 70 CYS A 86 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 2 2 Bytes