Header list of 1jxc.pdb file
Complete list - 23 202 Bytes
HEADER HYDROLASE INHIBITOR 06-SEP-01 1JXC TITLE MINIMIZED NMR STRUCTURE OF ATT, AN ARABIDOPSIS TRYPSIN/CHYMOTRYPSIN TITLE 2 INHIBITOR COMPND MOL_ID: 1; COMPND 2 MOLECULE: PUTATIVE TRYPSIN INHIBITOR ATTI-2; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA; SOURCE 3 ORGANISM_COMMON: THALE CRESS; SOURCE 4 ORGANISM_TAXID: 3702; SOURCE 5 GENE: ATTP; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)/PLYSS; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PSNHISATT KEYWDS ATT, TRYPSIN INHIBITOR, CHYMOTRYPSIN INHIBITOR, STRUCTURAL GENOMICS, KEYWDS 2 PROTEIN STRUCTURE INITIATIVE, CENTER FOR EUKARYOTIC STRUCTURAL KEYWDS 3 GENOMICS, CESG, HYDROLASE INHIBITOR EXPDTA SOLUTION NMR MDLTYP MINIMIZED AVERAGE AUTHOR Q.ZHAO,Y.K.CHAE,J.L.MARKLEY,CENTER FOR EUKARYOTIC STRUCTURAL GENOMICS AUTHOR 2 (CESG) REVDAT 5 23-FEB-22 1JXC 1 REMARK REVDAT 4 24-FEB-09 1JXC 1 VERSN REVDAT 3 12-FEB-08 1JXC 1 REMARK REVDAT 2 01-FEB-05 1JXC 1 AUTHOR KEYWDS REMARK REVDAT 1 07-JAN-03 1JXC 0 JRNL AUTH Q.ZHAO,Y.K.CHAE,J.L.MARKLEY JRNL TITL NMR SOLUTION STRUCTURE OF ATTP, AN ARABIDOPSIS THALIANA JRNL TITL 2 TRYPSIN INHIBITOR JRNL REF BIOCHEMISTRY V. 41 12284 2002 JRNL REFN ISSN 0006-2960 JRNL PMID 12369816 JRNL DOI 10.1021/BI025702A REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : DYANA 1.5, DYANA 1.5 REMARK 3 AUTHORS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1JXC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-SEP-01. REMARK 100 THE DEPOSITION ID IS D_1000014295. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 5.0 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : 1MM 15N 13C ATT 50 MM SODIUM REMARK 210 PERDEUTERATED ACETATE 0.1 MM DSS; REMARK 210 1MM 15N ATT 50 MM SODIUM REMARK 210 PERDEUTERATED ACETATE 0.1 MM DSS; REMARK 210 1MM ATT 50 MM SODIUM REMARK 210 PERDEUTERATED ACETATE 0.1 MM DSS; REMARK 210 1MM ATT 50 MM SODIUM REMARK 210 PERDEUTERATED ACETATE 0.1 MM DSS REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : HNCA; HN(CO)CA; HNCACB; C(CO)NH REMARK 210 SE; 3D_15N-SEPARATED_NOESY; 3D_ REMARK 210 13C-SEPARATED_NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 750 MHZ REMARK 210 SPECTROMETER MODEL : DMX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : XWINNMR, FELIX, SPARKY, XEASY REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS 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 PRO A 2 -169.31 -74.96 REMARK 500 ILE A 4 60.93 -69.12 REMARK 500 GLN A 7 113.09 61.04 REMARK 500 ASN A 9 52.66 -162.12 REMARK 500 GLU A 10 -67.86 -108.59 REMARK 500 TYR A 15 119.49 178.55 REMARK 500 ASP A 18 28.94 -153.11 REMARK 500 CYS A 24 -159.94 -69.34 REMARK 500 ALA A 25 120.60 81.20 REMARK 500 ARG A 27 -48.43 -140.40 REMARK 500 LYS A 41 -100.27 60.68 REMARK 500 ALA A 43 118.16 -179.26 REMARK 500 TRP A 50 -95.12 -43.79 REMARK 500 GLN A 52 88.54 153.70 REMARK 500 SER A 54 39.44 173.74 REMARK 500 VAL A 56 -168.29 -103.25 REMARK 500 CYS A 63 -76.97 -57.21 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 5056 RELATED DB: BMRB REMARK 900 CHEMICAL SHIFT ASSIGNMENT REMARK 900 RELATED ID: GO.9161 RELATED DB: TARGETDB DBREF 1JXC A 1 68 UNP Q42328 ITI2_ARATH 22 89 SEQADV 1JXC CYS A 1 UNP Q42328 VAL 22 SEE REMARK 999 SEQRES 1 A 68 CYS PRO GLU ILE GLU ALA GLN GLY ASN GLU CYS LEU LYS SEQRES 2 A 68 GLU TYR GLY GLY ASP VAL GLY PHE GLY PHE CYS ALA PRO SEQRES 3 A 68 ARG ILE PHE PRO THR ILE CYS TYR THR ARG CYS ARG GLU SEQRES 4 A 68 ASN LYS GLY ALA LYS GLY GLY ARG CYS ARG TRP GLY GLN SEQRES 5 A 68 GLY SER ASN VAL LYS CYS LEU CYS ASP PHE CYS GLY ASP SEQRES 6 A 68 THR PRO GLN HELIX 1 1 THR A 31 LYS A 41 1 11 SHEET 1 A 2 GLY A 45 CYS A 48 0 SHEET 2 A 2 CYS A 58 ASP A 61 -1 O LEU A 59 N ARG A 47 SSBOND 1 CYS A 11 CYS A 63 1555 1555 2.11 SSBOND 2 CYS A 24 CYS A 48 1555 1555 2.02 SSBOND 3 CYS A 33 CYS A 58 1555 1555 1.97 SSBOND 4 CYS A 37 CYS A 60 1555 1555 2.10 CRYST1 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 - 23 202 Bytes