Header list of 3cti.pdb file
Complete list - 16 20 Bytes
HEADER PROTEINASE INHIBITOR (TRYPSIN) 27-MAR-91 3CTI TITLE RELAXATION MATRIX REFINEMENT OF THE SOLUTION STRUCTURE OF SQUASH TITLE 2 TRYPSIN INHIBITOR COMPND MOL_ID: 1; COMPND 2 MOLECULE: TRYPSIN INHIBITOR; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: CUCURBITA MAXIMA; SOURCE 3 ORGANISM_COMMON: WINTER SQUASH; SOURCE 4 ORGANISM_TAXID: 3661 KEYWDS PROTEINASE INHIBITOR (TRYPSIN) EXPDTA SOLUTION NMR NUMMDL 6 AUTHOR M.NILGES,J.HABAZETTL,A.T.BRUENGER,T.A.HOLAK REVDAT 5 16-MAR-22 3CTI 1 REMARK REVDAT 4 24-FEB-09 3CTI 1 VERSN REVDAT 3 01-APR-03 3CTI 1 JRNL REVDAT 2 15-OCT-92 3CTI 2 CONECT REVDAT 1 15-APR-92 3CTI 0 JRNL AUTH M.NILGES,J.HABAZETTL,A.T.BRUNGER,T.A.HOLAK JRNL TITL RELAXATION MATRIX REFINEMENT OF THE SOLUTION STRUCTURE OF JRNL TITL 2 SQUASH TRYPSIN INHIBITOR. JRNL REF J.MOL.BIOL. V. 219 499 1991 JRNL REFN ISSN 0022-2836 JRNL PMID 2051485 JRNL DOI 10.1016/0022-2836(91)90189-D REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH T.A.HOLAK,D.GONDOL,J.OTLEWSKI,T.WILUSZ REMARK 1 TITL DETERMINATION OF THE COMPLETE THREE-DIMENSIONAL STRUCTURE OF REMARK 1 TITL 2 THE TRYPSIN INHIBITOR FROM SQUASH SEEDS IN AQUEOUS SOLUTION REMARK 1 TITL 3 BY NUCLEAR MAGNETIC RESONANCE AND A COMBINATION OF DISTANCE REMARK 1 TITL 4 GEOMETRY AND DYNAMICAL SIMULATED ANNEALING REMARK 1 REF J.MOL.BIOL. V. 210 635 1989 REMARK 1 REFN ISSN 0022-2836 REMARK 1 REFERENCE 2 REMARK 1 AUTH T.A.HOLAK,W.BODE,R.HUBER,J.OTLEWSKI,T.WILUSZ REMARK 1 TITL NUCLEAR MAGNETIC RESONANCE SOLUTION AND X-RAY STRUCTURES OF REMARK 1 TITL 2 SQUASH TRYPSIN INHIBITOR EXHIBIT THE SAME CONFORMATION OF REMARK 1 TITL 3 THE PROTEINASE BINDING LOOP REMARK 1 REF J.MOL.BIOL. V. 210 649 1989 REMARK 1 REFN ISSN 0022-2836 REMARK 1 REFERENCE 3 REMARK 1 AUTH J.HABAZETTL,C.CIESLAR,H.OSCHKINAT,T.A.HOLAK REMARK 1 TITL 1H NMR ASSIGNMENTS OF SIDECHAIN CONFORMATIONS IN PROTEINS REMARK 1 TITL 2 USING A HIGH-DIMENSIONAL POTENTIAL IN THE SIMULATED REMARK 1 TITL 3 ANNEALING CALCULATIONS REMARK 1 REF FEBS LETT. V. 268 141 1990 REMARK 1 REFN ISSN 0014-5793 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR REMARK 3 AUTHORS : HAVEL,WUTHRICH (DISGEO), BRUNGER (X-PLOR) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 3CTI COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL. REMARK 100 THE DEPOSITION ID IS D_1000178927. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : NULL REMARK 210 PH : NULL REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL REMARK 210 SPECTROMETER FIELD STRENGTH : NULL REMARK 210 SPECTROMETER MODEL : NULL REMARK 210 SPECTROMETER MANUFACTURER : NULL REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NULL REMARK 210 METHOD USED : NULL REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL REMARK 210 CONFORMERS, NUMBER SUBMITTED : 6 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: 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 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 1 TYR A 27 CB - CG - CD2 ANGL. DEV. = 3.6 DEGREES REMARK 500 1 TYR A 27 CB - CG - CD1 ANGL. DEV. = -3.7 DEGREES REMARK 500 3 TYR A 27 CB - CG - CD2 ANGL. DEV. = 3.7 DEGREES REMARK 500 3 TYR A 27 CB - CG - CD1 ANGL. DEV. = -3.8 DEGREES REMARK 500 4 TYR A 27 CB - CG - CD1 ANGL. DEV. = -3.7 DEGREES REMARK 500 5 TYR A 27 CB - CG - CD2 ANGL. DEV. = 3.6 DEGREES REMARK 500 5 TYR A 27 CB - CG - CD1 ANGL. DEV. = -3.7 DEGREES 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 CYS A 3 85.54 -153.05 REMARK 500 1 LEU A 7 103.69 -45.93 REMARK 500 1 ALA A 18 -163.11 50.11 REMARK 500 2 MET A 8 138.00 -179.95 REMARK 500 2 SER A 14 1.71 -61.82 REMARK 500 2 ALA A 18 -166.20 60.24 REMARK 500 2 GLU A 19 27.19 -79.78 REMARK 500 2 HIS A 25 0.23 -62.54 REMARK 500 3 LEU A 7 101.15 -43.15 REMARK 500 3 ALA A 18 -163.59 57.92 REMARK 500 3 HIS A 25 -9.09 -56.92 REMARK 500 4 LEU A 7 100.58 -33.06 REMARK 500 4 ALA A 18 -160.38 53.22 REMARK 500 4 HIS A 25 -6.53 -58.78 REMARK 500 5 LEU A 7 95.48 -43.57 REMARK 500 5 ALA A 18 -161.29 56.10 REMARK 500 6 LEU A 7 96.39 -34.00 REMARK 500 6 LEU A 17 173.15 -44.22 REMARK 500 6 ALA A 18 -166.39 63.20 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 1 ARG A 1 0.18 SIDE CHAIN REMARK 500 1 ARG A 5 0.29 SIDE CHAIN REMARK 500 2 ARG A 1 0.29 SIDE CHAIN REMARK 500 2 ARG A 5 0.23 SIDE CHAIN REMARK 500 3 ARG A 1 0.15 SIDE CHAIN REMARK 500 3 ARG A 5 0.31 SIDE CHAIN REMARK 500 4 ARG A 1 0.30 SIDE CHAIN REMARK 500 4 ARG A 5 0.22 SIDE CHAIN REMARK 500 4 TYR A 27 0.07 SIDE CHAIN REMARK 500 5 ARG A 1 0.26 SIDE CHAIN REMARK 500 5 ARG A 5 0.26 SIDE CHAIN REMARK 500 6 ARG A 1 0.12 SIDE CHAIN REMARK 500 6 ARG A 5 0.14 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL DBREF 3CTI A 1 29 UNP P01074 ITR1_CUCMA 1 29 SEQRES 1 A 29 ARG VAL CYS PRO ARG ILE LEU MET GLU CYS LYS LYS ASP SEQRES 2 A 29 SER ASP CYS LEU ALA GLU CYS VAL CYS LEU GLU HIS GLY SEQRES 3 A 29 TYR CYS GLY HELIX 1 H1 ASP A 13 ASP A 15 5 3 SSBOND 1 CYS A 3 CYS A 20 1555 1555 2.02 SSBOND 2 CYS A 10 CYS A 22 1555 1555 2.02 SSBOND 3 CYS A 16 CYS A 28 1555 1555 2.02 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 - 16 20 Bytes