Header list of 1qh2.pdb file
Complete list - 2 202 Bytes
HEADER HYDROLASE INHIBITOR 11-MAY-99 1QH2 TITLE CHYMOTRYPSIN INHIBITOR (C2) FROM NICOTIANA ALATA COMPND MOL_ID: 1; COMPND 2 MOLECULE: PROTEIN (TRYPSIN INHIBITOR C2); COMPND 3 CHAIN: A; COMPND 4 MOL_ID: 2; COMPND 5 MOLECULE: PROTEIN (TRYPSIN INHIBITOR C2); COMPND 6 CHAIN: B SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: NICOTIANA ALATA; SOURCE 3 ORGANISM_COMMON: PERSIAN TOBACCO; SOURCE 4 ORGANISM_TAXID: 4087; SOURCE 5 ORGAN: STIGMA; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: NICOTIANA ALATA; SOURCE 8 ORGANISM_COMMON: PERSIAN TOBACCO; SOURCE 9 ORGANISM_TAXID: 4087; SOURCE 10 ORGAN: STIGMA KEYWDS PROTEINASE INHIBITOR (CHYMOTRYPSIN), SERINE PROTEINASE INHIBITOR, KEYWDS 2 POTATO II TRYPSIN INHIBITOR, NICOTIANA ALATA, HYDROLASE INHIBITOR EXPDTA SOLUTION NMR AUTHOR M.C.S.LEE,M.J.SCANLON,M.A.ANDERSON,D.J.CRAIK REVDAT 5 02-MAR-22 1QH2 1 REMARK REVDAT 4 24-FEB-09 1QH2 1 VERSN REVDAT 3 01-APR-03 1QH2 1 JRNL REVDAT 2 27-DEC-99 1QH2 1 JRNL REVDAT 1 24-MAY-99 1QH2 0 JRNL AUTH M.C.LEE,M.J.SCANLON,D.J.CRAIK,M.A.ANDERSON JRNL TITL A NOVEL TWO-CHAIN PROTEINASE INHIBITOR GENERATED BY JRNL TITL 2 CIRCULARIZATION OF A MULTIDOMAIN PRECURSOR PROTEIN. JRNL REF NAT.STRUCT.BIOL. V. 6 526 1999 JRNL REFN ISSN 1072-8368 JRNL PMID 10360353 JRNL DOI 10.1038/9293 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH K.J.NIELSEN,R.L.HEATH,M.A.ANDERSON,D.J.CRAIK REMARK 1 TITL THE THREE-DIMENSIONAL SOLUTION STRUCTURE BY 1H NMR OF A REMARK 1 TITL 2 6-KDA PROTEINASE INHIBITOR ISOLATED FROM THE STIGMA OF REMARK 1 TITL 3 NICOTIANA ALATA REMARK 1 REF J.MOL.BIOL. V. 242 231 1994 REMARK 1 REFN ISSN 0022-2836 REMARK 1 DOI 10.1006/JMBI.1994.1575 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.851 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1QH2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-MAY-99. REMARK 100 THE DEPOSITION ID IS D_1000001033. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 313 REMARK 210 PH : 5.2 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : 10% D2O/90% H2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; TOCSY; DQFCOSY; ECOSY REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ REMARK 210 SPECTROMETER MODEL : DRX750 REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : DYANA, X-PLOR REMARK 210 METHOD USED : SIMULATED 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: 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 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 -166.44 56.41 REMARK 500 LEU A 5 -126.31 -135.01 REMARK 500 ASN A 6 92.12 51.97 REMARK 500 CYS A 7 51.86 -160.47 REMARK 500 ASP A 8 130.24 61.01 REMARK 500 ARG A 10 -10.09 -152.55 REMARK 500 ILE A 11 170.25 -59.65 REMARK 500 ALA A 12 -67.99 -131.49 REMARK 500 CYS B 3 0.03 -165.20 REMARK 500 THR B 4 118.68 73.84 REMARK 500 ASN B 5 135.41 118.34 REMARK 500 CYS B 6 15.11 -55.90 REMARK 500 ALA B 8 29.97 -157.91 REMARK 500 LYS B 11 65.47 86.23 REMARK 500 ASP B 18 -70.43 45.45 REMARK 500 ILE B 23 -42.93 -143.83 REMARK 500 GLU B 25 43.39 -84.08 REMARK 500 GLU B 27 -1.67 152.73 REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: S1 REMARK 800 EVIDENCE_CODE: AUTHOR REMARK 800 SITE_DESCRIPTION: CHYMOTRYPSIN REACTIVE SITE REMARK 999 REMARK 999 SEQUENCE REMARK 999 SEQUENCE REFERENCE: A.H.ATKINSON,R.L.HEATH, R.L.SIMPSON, REMARK 999 A.C.CLARKE,M.A.ANDERSON, PLANT CELL, 5, 203-213. DBREF 1QH2 A 1 18 UNP Q40378 Q40378_NICAL 30 47 DBREF 1QH2 B 1 28 UNP Q40378 Q40378_NICAL 345 372 SEQRES 1 A 18 LYS ALA CYS THR LEU ASN CYS ASP PRO ARG ILE ALA TYR SEQRES 2 A 18 GLY VAL CYS PRO ARG SEQRES 1 B 28 ARG ILE CYS THR ASN CYS CYS ALA GLY LYS LYS GLY CYS SEQRES 2 B 28 LYS TYR PHE SER ASP ASP GLY THR PHE ILE CYS GLU GLY SEQRES 3 B 28 GLU SER SHEET 1 A 2 TYR A 13 VAL A 15 0 SHEET 2 A 2 LYS B 14 PHE B 16 -1 N PHE B 16 O TYR A 13 SSBOND 1 CYS A 3 CYS B 7 1555 1555 2.02 SSBOND 2 CYS A 7 CYS B 3 1555 1555 2.02 SSBOND 3 CYS A 16 CYS B 13 1555 1555 2.02 SSBOND 4 CYS B 6 CYS B 24 1555 1555 2.02 SITE 1 S1 2 LEU A 5 ASN A 6 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 - 2 202 Bytes