Header list of 1jbn.pdb file
Complete list - 28 20 Bytes
HEADER PROTEIN BINDING 06-JUN-01 1JBN
TITLE SOLUTION STRUCTURE OF AN ACYCLIC PERMUTANT OF SFTI-1, A TRYPSIN
TITLE 2 INHIBITOR FROM SUNFLOWER SEEDS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYCLIC TRYPSIN INHIBITOR;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: SFTI-1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 ORGANISM_SCIENTIFIC: HELIANTHUS ANNUUS;
SOURCE 4 ORGANISM_TAXID: 4232;
SOURCE 5 OTHER_DETAILS: ACIRCULAR PERMUTATION OF A NATURALLY OCCURRING
SOURCE 6 CIRCULAR PEPTIDE FROM SUNFLOWER SEEDS.
KEYWDS BETA SHEET, 1 DISULFIDE BRIDGE, LINEAR BACKBONE, 14/1-LSFTI-1,
KEYWDS 2 PROTEIN BINDING
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR M.L.J.KORSINCZKY,H.J.SCHIRRA,K.J.ROSENGREN,J.WEST,B.A.CONDIE,L.OTVOS,
AUTHOR 2 M.A.ANDERSON,D.J.CRAIK
REVDAT 7 28-DEC-16 1JBN 1 TITLE
REVDAT 6 13-JAN-16 1JBN 1 REMARK VERSN
REVDAT 5 16-FEB-11 1JBN 1 DBREF
REVDAT 4 24-FEB-09 1JBN 1 VERSN
REVDAT 3 01-APR-03 1JBN 1 JRNL
REVDAT 2 25-DEC-02 1JBN 1 REMARK
REVDAT 1 22-AUG-01 1JBN 0
JRNL AUTH M.L.KORSINCZKY,H.J.SCHIRRA,K.J.ROSENGREN,J.WEST,B.A.CONDIE,
JRNL AUTH 2 L.OTVOS,M.A.ANDERSON,D.J.CRAIK
JRNL TITL SOLUTION STRUCTURES BY 1H NMR OF THE NOVEL CYCLIC TRYPSIN
JRNL TITL 2 INHIBITOR SFTI-1 FROM SUNFLOWER SEEDS AND AN ACYCLIC
JRNL TITL 3 PERMUTANT.
JRNL REF J.MOL.BIOL. V. 311 579 2001
JRNL REFN ISSN 0022-2836
JRNL PMID 11493011
JRNL DOI 10.1006/JMBI.2001.4887
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:
REMARK 3 162 DISTANCE CONSTRAINTS,
REMARK 3 73 SEQUENTIAL,
REMARK 3 18 MEDIUM RANGE,
REMARK 3 68 LONG RANGE,
REMARK 3 6 CHI1 ANGLE CONSTRAINTS,
REMARK 3 7 PHI ANGLE CONSTRAINTS
REMARK 4
REMARK 4 1JBN COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-JUN-01.
REMARK 100 THE RCSB ID CODE IS RCSB013592.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 273; 313
REMARK 210 PH : 4.5; 4.5
REMARK 210 IONIC STRENGTH : 20MM; 20MM
REMARK 210 PRESSURE : AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM 14/1-LSFTI-1; 1MM 14/1-LSFTI
REMARK 210 -1; 1MM 14/1-LSFTI-1
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; DQF-COSY; E-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : DMX; ARX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 2.6, CCNMR, X-PLOR 3.851
REMARK 210 METHOD USED : SIMULATED ANNEALING AND
REMARK 210 REFINEMENT WITH MODIFIED CSDX
REMARK 210 FORCE FIELD
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS,STRUCTURES
REMARK 210 WITH THE LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D
REMARK 210 HOMONUCLEAR TECHNIQUES.
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
REMARK 400 THE ACYCLIC TRYPSIN INHIBITOR IS POLYPEPTIDE, A MEMBER OF TRYPSIN
REMARK 400 INHIBITOR CLASS.
REMARK 400
REMARK 400 GROUP: 1
REMARK 400 NAME: ACYCLIC TRYPSIN INHIBITOR
REMARK 400 CHAIN: A
REMARK 400 COMPONENT_1: PEPTIDE LIKE POLYMER
REMARK 400 DESCRIPTION: NULL
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 O ARG A 2 H PHE A 12 1.55
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 3 THR A 4 -165.34 -67.47
REMARK 500 4 THR A 4 -160.61 -67.19
REMARK 500 5 THR A 4 -169.21 -67.89
REMARK 500 5 LYS A 5 45.70 -109.55
REMARK 500 5 PRO A 13 32.31 -73.02
REMARK 500 7 LYS A 5 40.23 -99.83
REMARK 500 8 THR A 4 -160.51 -67.84
REMARK 500 9 LYS A 5 38.83 -87.12
REMARK 500 12 LYS A 5 30.84 -82.48
REMARK 500 13 LYS A 5 32.01 -84.98
REMARK 500 14 THR A 4 -175.69 -67.35
REMARK 500 14 LYS A 5 43.32 -103.29
REMARK 500 15 THR A 4 -175.78 -67.14
REMARK 500 15 LYS A 5 43.27 -103.29
REMARK 500 16 THR A 4 -167.43 -71.11
REMARK 500 18 THR A 4 -164.17 -68.41
REMARK 500 19 THR A 4 -174.39 -64.96
REMARK 500 19 LYS A 5 43.43 -105.69
REMARK 500 20 LYS A 5 32.97 -84.91
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1JBL RELATED DB: PDB
REMARK 900 1JBL CONTAINS CYCLIC SFTI-1 (PARENT MOLECULE)
DBREF 1JBN A 1 14 UNP Q4GWU5 SFTI1_HELAN 1 14
SEQRES 1 A 14 GLY ARG CYS THR LYS SER ILE PRO PRO ILE CYS PHE PRO
SEQRES 2 A 14 ASP
SHEET 1 A 2 ARG A 2 CYS A 3 0
SHEET 2 A 2 CYS A 11 PHE A 12 -1 N PHE A 12 O ARG A 2
SSBOND 1 CYS A 3 CYS A 11 1555 1555 2.03
CISPEP 1 ILE A 7 PRO A 8 1 -0.45
CISPEP 2 ILE A 7 PRO A 8 2 -0.57
CISPEP 3 ILE A 7 PRO A 8 3 -0.68
CISPEP 4 ILE A 7 PRO A 8 4 -0.29
CISPEP 5 ILE A 7 PRO A 8 5 -0.43
CISPEP 6 ILE A 7 PRO A 8 6 -0.43
CISPEP 7 ILE A 7 PRO A 8 7 -0.59
CISPEP 8 ILE A 7 PRO A 8 8 -0.46
CISPEP 9 ILE A 7 PRO A 8 9 -0.57
CISPEP 10 ILE A 7 PRO A 8 10 -0.51
CISPEP 11 ILE A 7 PRO A 8 11 -0.66
CISPEP 12 ILE A 7 PRO A 8 12 -0.51
CISPEP 13 ILE A 7 PRO A 8 13 -0.43
CISPEP 14 ILE A 7 PRO A 8 14 -0.40
CISPEP 15 ILE A 7 PRO A 8 15 -0.45
CISPEP 16 ILE A 7 PRO A 8 16 -0.53
CISPEP 17 ILE A 7 PRO A 8 17 -0.64
CISPEP 18 ILE A 7 PRO A 8 18 -0.51
CISPEP 19 ILE A 7 PRO A 8 19 -0.46
CISPEP 20 ILE A 7 PRO A 8 20 -0.45
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 - 28 20 Bytes