Click here to see the 3D structure Header list of 1z7r.pdb file

Complete list - 26 20 Bytes
HEADER ELECTRON TRANSPORT 26-MAR-05 1Z7R TITLE SOLUTION STRUCTURE OF REDUCED GLUTAREDOXIN C1 FROM POPULUS TREMULA X TITLE 2 TREMULOIDES COMPND MOL_ID: 1; COMPND 2 MOLECULE: GLUTAREDOXIN; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: GLUTAREDOXIN C1; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: POPULUS TREMULA X POPULUS TREMULOIDES; SOURCE 3 ORGANISM_TAXID: 47664; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET3D KEYWDS ELECTRON TRANSPORT EXPDTA SOLUTION NMR MDLTYP MINIMIZED AVERAGE AUTHOR Y.FENG,N.ZHONG,N.ROUHIER,J.P.JACQUOT,B.XIA REVDAT 4 26-FEB-20 1Z7R 1 REMARK SEQADV REVDAT 3 24-FEB-09 1Z7R 1 VERSN REVDAT 2 25-JUL-06 1Z7R 1 JRNL AUTHOR REVDAT 1 28-MAR-06 1Z7R 0 JRNL AUTH Y.FENG,N.ZHONG,N.ROUHIER,T.HASE,M.KUSUNOKI,J.P.JACQUOT, JRNL AUTH 2 C.JIN,B.XIA JRNL TITL STRUCTURAL INSIGHT INTO POPLAR GLUTAREDOXIN C1 WITH A JRNL TITL 2 BRIDGING IRON-SULFUR CLUSTER AT THE ACTIVE SITE JRNL REF BIOCHEMISTRY V. 45 7998 2006 JRNL REFN ISSN 0006-2960 JRNL PMID 16800625 JRNL DOI 10.1021/BI060444T REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CYANA 1.0.6, AMBER 7 REMARK 3 AUTHORS : GUNTERT, P. (CYANA), CASE, D. A. (AMBER) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: CYS 31 IS PRESENT AS THE THIOLATE WITH REMARK 3 A NEGATIVE CHARGE ON THE SULFUR. REMARK 4 REMARK 4 1Z7R COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 29-MAR-05. REMARK 100 THE DEPOSITION ID IS D_1000032404. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 293 REMARK 210 PH : 6.4 REMARK 210 IONIC STRENGTH : 40MM POTASSIUM PHOSPHATE REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1.1MM UNIFORMLY 13C/15N-LABELED REMARK 210 PROTEIN, 40MM POTASSIUM REMARK 210 PHOSPHATE BUFFER, 90% H2O/10% REMARK 210 D2O, 40MM DTT, 0.01% NAN3 AND REMARK 210 0.01% DSS, PROTEASE INHIBITOR REMARK 210 COCKTAIL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C REMARK 210 -SEPARATED_NOESY; 3D_13C- REMARK 210 SEPARATED_NOESY IN AROMATIC REMARK 210 REGION REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ REMARK 210 SPECTROMETER MODEL : AVANCE REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRVIEW 5.2.2, NMRPIPE 2.3 REMARK 210 METHOD USED : MOLECULAR DYNAMICS, SIMULATED REMARK 210 ANNEALING 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 ALA A 2 -17.57 138.18 REMARK 500 GLN A 116 155.44 70.90 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 6410 RELATED DB: BMRB REMARK 900 CHEMICAL SHIFT ASSIGNMENT REMARK 900 RELATED ID: 1Z7P RELATED DB: PDB REMARK 900 ENSEMBLE DBREF 1Z7R A 3 112 UNP Q5PSJ1 Q5PSJ1_9ROSI 12 121 SEQADV 1Z7R MET A 1 UNP Q5PSJ1 CLONING ARTIFACT SEQADV 1Z7R ALA A 2 UNP Q5PSJ1 CLONING ARTIFACT SEQADV 1Z7R ASN A 113 UNP Q5PSJ1 SEE REMARK 999 SEQADV 1Z7R PRO A 114 UNP Q5PSJ1 SEE REMARK 999 SEQADV 1Z7R ALA A 115 UNP Q5PSJ1 SEE REMARK 999 SEQADV 1Z7R GLN A 116 UNP Q5PSJ1 SEE REMARK 999 SEQADV 1Z7R LEU A 117 UNP Q5PSJ1 SEE REMARK 999 SEQRES 1 A 117 MET ALA SER LYS GLN GLU LEU ASP ALA ALA LEU LYS LYS SEQRES 2 A 117 ALA LYS GLU LEU ALA SER SER ALA PRO VAL VAL VAL PHE SEQRES 3 A 117 SER LYS THR TYR CYS GLY TYR CYS ASN ARG VAL LYS GLN SEQRES 4 A 117 LEU LEU THR GLN VAL GLY ALA SER TYR LYS VAL VAL GLU SEQRES 5 A 117 LEU ASP GLU LEU SER ASP GLY SER GLN LEU GLN SER ALA SEQRES 6 A 117 LEU ALA HIS TRP THR GLY ARG GLY THR VAL PRO ASN VAL SEQRES 7 A 117 PHE ILE GLY GLY LYS GLN ILE GLY GLY CYS ASP THR VAL SEQRES 8 A 117 VAL GLU LYS HIS GLN ARG ASN GLU LEU LEU PRO LEU LEU SEQRES 9 A 117 GLN ASP ALA ALA ALA THR ALA LYS ASN PRO ALA GLN LEU HELIX 1 1 ALA A 2 SER A 20 1 19 HELIX 2 2 CYS A 31 GLY A 45 1 15 HELIX 3 3 ASP A 58 GLY A 71 1 14 HELIX 4 4 CYS A 88 ARG A 97 1 10 HELIX 5 5 GLU A 99 ALA A 107 1 9 SHEET 1 A 4 LYS A 49 GLU A 52 0 SHEET 2 A 4 VAL A 23 SER A 27 1 N SER A 27 O VAL A 51 SHEET 3 A 4 ASN A 77 ILE A 80 -1 O PHE A 79 N VAL A 24 SHEET 4 A 4 LYS A 83 GLY A 87 -1 O ILE A 85 N VAL A 78 CISPEP 1 VAL A 75 PRO A 76 0 -10.09 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 - 26 20 Bytes