Header list of 2cti.pdb file
Complete list - 9 20 Bytes
HEADER PROTEINASE INHIBITOR (TRYPSIN) 28-AUG-90 2CTI
TITLE DETERMINATION OF THE COMPLETE THREE-DIMENSIONAL STRUCTURE OF THE
TITLE 2 TRYPSIN INHIBITOR FROM SQUASH SEEDS IN AQUEOUS SOLUTION BY NUCLEAR
TITLE 3 MAGNETIC RESONANCE AND A COMBINATION OF DISTANCE GEOMETRY AND
TITLE 4 DYNAMICAL SIMULATED ANNEALING
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 5
AUTHOR T.A.HOLAK,D.GONDOL,J.OTLEWSKI,T.WILUSZ
REVDAT 3 09-MAR-22 2CTI 1 REMARK
REVDAT 2 24-FEB-09 2CTI 1 VERSN
REVDAT 1 15-JAN-92 2CTI 0
JRNL AUTH T.A.HOLAK,D.GONDOL,J.OTLEWSKI,T.WILUSZ
JRNL TITL DETERMINATION OF THE COMPLETE THREE-DIMENSIONAL STRUCTURE OF
JRNL TITL 2 THE TRYPSIN INHIBITOR FROM SQUASH SEEDS IN AQUEOUS SOLUTION
JRNL TITL 3 BY NUCLEAR MAGNETIC RESONANCE AND A COMBINATION OF DISTANCE
JRNL TITL 4 GEOMETRY AND DYNAMICAL SIMULATED ANNEALING.
JRNL REF J.MOL.BIOL. V. 210 635 1989
JRNL REFN ISSN 0022-2836
JRNL PMID 2614837
JRNL DOI 10.1016/0022-2836(89)90137-X
REMARK 1
REMARK 1 REFERENCE 1
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 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DISGEO, X-PLOR
REMARK 3 AUTHORS : HAVEL,WUTHRICH (DISGEO), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2CTI 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_1000177958.
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 : 5
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: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 1 HIS A 25 CG HIS A 25 ND1 -0.095
REMARK 500 2 HIS A 25 CG HIS A 25 ND1 -0.095
REMARK 500 3 HIS A 25 CG HIS A 25 ND1 -0.095
REMARK 500 4 HIS A 25 CG HIS A 25 ND1 -0.096
REMARK 500 5 HIS A 25 CG HIS A 25 ND1 -0.095
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 ALA A 18 -157.26 51.55
REMARK 500 2 CYS A 3 85.29 -155.49
REMARK 500 2 ALA A 18 -162.72 54.17
REMARK 500 3 ALA A 18 -154.39 52.97
REMARK 500 4 CYS A 3 84.67 -150.41
REMARK 500 4 ALA A 18 -150.60 52.72
REMARK 500 5 LEU A 7 71.43 -107.41
REMARK 500 5 ALA A 18 -152.17 52.95
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 0.15 SIDE CHAIN
REMARK 500 1 ARG A 5 0.32 SIDE CHAIN
REMARK 500 2 ARG A 1 0.21 SIDE CHAIN
REMARK 500 2 ARG A 5 0.13 SIDE CHAIN
REMARK 500 3 ARG A 1 0.32 SIDE CHAIN
REMARK 500 3 ARG A 5 0.31 SIDE CHAIN
REMARK 500 4 ARG A 1 0.22 SIDE CHAIN
REMARK 500 4 ARG A 5 0.32 SIDE CHAIN
REMARK 500 5 ARG A 1 0.29 SIDE CHAIN
REMARK 500 5 ARG A 5 0.32 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1CTI RELATED DB: PDB
DBREF 2CTI 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 1 LYS A 12 CYS A 16 5 5
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 2.01
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 - 9 20 Bytes