Header list of 1gm2.pdb file
Complete list - 29 20 Bytes
HEADER HYDROLASE INHIBITOR 08-SEP-01 1GM2 TITLE THE INDEPENDENT STRUCTURE OF THE ANTITRYPTIC REACTIVE SITE LOOP OF TITLE 2 BOWMAN-BIRK INHIBITOR AND SUNFLOWER TRYPSIN INHIBITOR-1 COMPND MOL_ID: 1; COMPND 2 MOLECULE: BOWMAN-BIRK INHIBITOR DERIVED PEPTIDE; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: ANTITRYPTIC REACTIVE SITE LOOP; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 SYNTHETIC: YES; SOURCE 3 ORGANISM_SCIENTIFIC: MACROTYLOMA AXILLARE; SOURCE 4 ORGANISM_TAXID: 3876 KEYWDS BOWMAN-BIRK INHIBITOR PROTEIN MIMETIC, SUNFLOWER TRYPSIN INHIBITOR-1 KEYWDS 2 (SFTI-1) MIMETIC, TRYPSIN INHIBITOR, TYPE VIB BETA-TURN PEPTIDE, KEYWDS 3 HYDROLASE INHIBITOR EXPDTA SOLUTION NMR NUMMDL 30 AUTHOR A.B.E.BRAUER,G.KELLY,S.J.MATTHEWS,R.J.LEATHERBARROW REVDAT 5 29-JUL-20 1GM2 1 SOURCE REVDAT 4 09-OCT-19 1GM2 1 JRNL REVDAT 3 13-JUL-11 1GM2 1 VERSN REVDAT 2 24-FEB-09 1GM2 1 VERSN REVDAT 1 29-AUG-02 1GM2 0 JRNL AUTH A.B.BRAUER,G.KELLY,S.J.MATTHEWS,R.J.LEATHERBARROW JRNL TITL THE (1)H-NMR SOLUTION STRUCTURE OF THE ANTITRYPTIC CORE JRNL TITL 2 PEPTIDE OF BOWMAN-BIRK INHIBITOR PROTEINS: A MINIMAL JRNL TITL 3 CANONICAL LOOP. JRNL REF J.BIOMOL.STRUCT.DYN. V. 20 59 2002 JRNL REFN ISSN 0739-1102 JRNL PMID 12144352 JRNL DOI 10.1080/07391102.2002.10506822 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH A.B.E.BRAUER,G.J.DOMINGO,R.M.COOKE,S.J.MATTHEWS, REMARK 1 AUTH 2 R.J.LEATHERBARROW REMARK 1 TITL A CONSERVED CIS PEPTIDE BOND IS NECESSARY FOR THE ACTIVITY REMARK 1 TITL 2 OF BOWMAN-BIRK INHIBITOR PROTEIN REMARK 1 REF BIOCHEMISTRY V. 41 10608 2002 REMARK 1 REFN ISSN 0006-2960 REMARK 1 PMID 12186545 REMARK 1 DOI 10.1021/BI026050T REMARK 1 REFERENCE 2 REMARK 1 AUTH A.B.E.BRAUER,G.KELLY,J.D.MCBRIDE,R.M.COOKE,S.J.MATTHEWS, REMARK 1 AUTH 2 R.J.LEATHERBARROW REMARK 1 TITL THE BOWMAN-BIRK INHIBITOR REACTIVE SITE LOOP REPRESENTS AN REMARK 1 TITL 2 INDEPENDENT STRUCTURAL BETA-HAIRPIN MOTIF REMARK 1 REF J.MOL.BIOL. V. 306 799 2001 REMARK 1 REFN ISSN 0022-2836 REMARK 1 PMID 11243789 REMARK 1 DOI 10.1006/JMBI.2000.4410 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 1GM2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-SEP-01. REMARK 100 THE DEPOSITION ID IS D_1290008550. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 3.8 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : TOCSY; COSY; NOESY; ROESY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : AMX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NULL REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 300 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30 REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING 1H-NMR. 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 400 REMARK 400 COMPOUND REMARK 400 TERMINAL RESIDUES ARE MUTATED REALTIVE TO WILD TYPE SEQUENCE 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 3 LYS A 4 39.46 -97.80 REMARK 500 5 LYS A 4 39.89 -97.33 REMARK 500 8 THR A 3 -177.88 -60.06 REMARK 500 8 LYS A 4 30.25 -99.68 REMARK 500 9 LYS A 4 44.89 -97.07 REMARK 500 10 LYS A 4 31.93 -99.60 REMARK 500 11 THR A 3 -172.41 -69.71 REMARK 500 12 LYS A 4 37.01 -98.54 REMARK 500 13 LYS A 4 30.65 -99.62 REMARK 500 14 LYS A 4 34.89 -99.44 REMARK 500 15 THR A 3 -173.46 -67.70 REMARK 500 15 LYS A 4 55.39 -118.90 REMARK 500 16 THR A 3 -172.99 -60.73 REMARK 500 17 LYS A 4 50.50 -91.85 REMARK 500 18 THR A 3 -177.54 -60.41 REMARK 500 19 THR A 3 175.20 -59.89 REMARK 500 19 LYS A 4 59.19 -95.88 REMARK 500 24 LYS A 4 32.79 -98.78 REMARK 500 26 LYS A 4 39.24 -99.02 REMARK 500 27 LYS A 4 41.79 -104.15 REMARK 500 28 THR A 3 -177.37 -60.08 REMARK 500 29 LYS A 4 37.22 -98.79 REMARK 500 REMARK 500 REMARK: NULL DBREF 1GM2 A 1 1 PDB 1GM2 1GM2 1 1 DBREF 1GM2 A 2 10 UNP P01059 P01059 21 29 DBREF 1GM2 A 11 11 PDB 1GM2 1GM2 11 11 SEQRES 1 A 11 SER CYS THR LYS SER ILE PRO PRO GLN CYS TYR SSBOND 1 CYS A 2 CYS A 10 1555 1555 2.03 CISPEP 1 ILE A 6 PRO A 7 1 0.10 CISPEP 2 ILE A 6 PRO A 7 2 0.12 CISPEP 3 ILE A 6 PRO A 7 3 0.00 CISPEP 4 ILE A 6 PRO A 7 4 0.01 CISPEP 5 ILE A 6 PRO A 7 5 0.04 CISPEP 6 ILE A 6 PRO A 7 6 0.12 CISPEP 7 ILE A 6 PRO A 7 7 0.09 CISPEP 8 ILE A 6 PRO A 7 8 0.14 CISPEP 9 ILE A 6 PRO A 7 9 0.26 CISPEP 10 ILE A 6 PRO A 7 10 -0.08 CISPEP 11 ILE A 6 PRO A 7 11 0.01 CISPEP 12 ILE A 6 PRO A 7 12 0.03 CISPEP 13 ILE A 6 PRO A 7 13 0.12 CISPEP 14 ILE A 6 PRO A 7 14 0.19 CISPEP 15 ILE A 6 PRO A 7 15 0.05 CISPEP 16 ILE A 6 PRO A 7 16 0.04 CISPEP 17 ILE A 6 PRO A 7 17 0.12 CISPEP 18 ILE A 6 PRO A 7 18 0.02 CISPEP 19 ILE A 6 PRO A 7 19 0.02 CISPEP 20 ILE A 6 PRO A 7 20 0.04 CISPEP 21 ILE A 6 PRO A 7 21 0.10 CISPEP 22 ILE A 6 PRO A 7 22 0.03 CISPEP 23 ILE A 6 PRO A 7 23 -0.01 CISPEP 24 ILE A 6 PRO A 7 24 0.10 CISPEP 25 ILE A 6 PRO A 7 25 0.05 CISPEP 26 ILE A 6 PRO A 7 26 0.07 CISPEP 27 ILE A 6 PRO A 7 27 0.00 CISPEP 28 ILE A 6 PRO A 7 28 -0.01 CISPEP 29 ILE A 6 PRO A 7 29 0.15 CISPEP 30 ILE A 6 PRO A 7 30 -0.06 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 - 29 20 Bytes