Header list of 1t9e.pdb file
Complete list - 25 20 Bytes
HEADER HYDROLASE/HYDROLASE INHIBITOR 16-MAY-04 1T9E
TITLE NMR SOLUTION STRUCTURE OF A DISULFIDE ANALOGUE OF THE CYCLIC SUNFLOWER
TITLE 2 TRYPSIN INHIBITOR SFTI-1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRYPSIN INHIBITOR 1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: SFTI-1;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 ORGANISM_SCIENTIFIC: HELIANTHUS ANNUUS;
SOURCE 4 ORGANISM_COMMON: COMMON SUNFLOWER;
SOURCE 5 ORGANISM_TAXID: 4232;
SOURCE 6 OTHER_DETAILS: THE PEPTIDE WAS SYNTHESIZED USING STANDARD SOLID
SOURCE 7 PHASE PEPTIDE SYNTHESIS METHODS USING BOC CHEMISTRY. THE PEPTIDE
SOURCE 8 BACKBONE WAS CYCLICIZED IN SOLUTION BY ADDITION OF HBTU AND DIEA
SOURCE 9 WHICH RESULTED IN THE FORMATION OF A PEPTIDE BOND BETWEEN D14 AND
SOURCE 10 G1. THE SEQUENCE OF THE PEPTIDE IS NATURALLY FOUND IN HELIANTHUS
SOURCE 11 ANNUS (SUNFLOWER)
KEYWDS SUNFLOWER TRYPSIN INHIBITOR, DISULFIDE MUTANT, HYDROLASE-HYDROLASE
KEYWDS 2 INHIBITOR COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR M.L.J.KORSINCZKY,R.J.CLARK,D.J.CRAIK
REVDAT 3 13-JUL-11 1T9E 1 VERSN
REVDAT 2 24-FEB-09 1T9E 1 VERSN
REVDAT 1 03-MAY-05 1T9E 0
JRNL AUTH M.L.J.KORSINCZKY,R.J.CLARK,D.J.CRAIK
JRNL TITL DISULFIDE BOND MUTAGENESIS AND THE STRUCTURE AND FUNCTION OF
JRNL TITL 2 THE HEAD-TO-TAIL MACROCYCLIC TRYPSIN INHIBITOR SFTI-1
JRNL REF BIOCHEMISTRY V. 44 1145 2005
JRNL REFN ISSN 0006-2960
JRNL PMID 15667208
JRNL DOI 10.1021/BI048297R
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
REMARK 3 AUTHORS : BRUNGER, ADAMS, CLORE, DELANO, GROS, GROSSE-
REMARK 3 KUNSTLEVE, JIANG, KUSZEWSKI, NILGES, PANNU, READ,
REMARK 3 RICE, SIMONSON, WARREN
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1T9E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-JUN-04.
REMARK 100 THE RCSB ID CODE IS RCSB022476.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 290
REMARK 210 PH : 4.5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 10 MM PEPTIDE IN 0.5 ML SOLVENT;
REMARK 210 10 MM PEPTIDE IN 0.5 ML SOLVENT
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : DQF-COSY; 2D TOCSY; 2D NOESY; E-
REMARK 210 COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ
REMARK 210 SPECTROMETER MODEL : DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 3.5, CNS 1.0
REMARK 210 METHOD USED : STRUCTURES WERE CALCULATED USING
REMARK 210 TORSION ANGLE DYNAMICS AND
REMARK 210 REFINED USING CARTESIAN DYNAMICS
REMARK 210 AND ENERGY MINIMIZATION IN
REMARK 210 SOLVENT USING CNS.
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
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 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 LYS A 5 47.90 -80.98
REMARK 500 2 LYS A 5 46.12 -80.55
REMARK 500 3 LYS A 5 49.91 -84.47
REMARK 500 4 LYS A 5 46.75 -82.71
REMARK 500 5 LYS A 5 48.14 -82.03
REMARK 500 5 PRO A 13 54.43 -66.72
REMARK 500 6 LYS A 5 49.26 -82.54
REMARK 500 8 LYS A 5 49.14 -84.21
REMARK 500 9 LYS A 5 43.96 -81.30
REMARK 500 10 LYS A 5 48.72 -84.16
REMARK 500 11 LYS A 5 48.68 -82.12
REMARK 500 12 LYS A 5 46.86 -82.41
REMARK 500 13 LYS A 5 49.33 -83.58
REMARK 500 14 LYS A 5 46.43 -81.14
REMARK 500 14 PRO A 13 53.57 -67.99
REMARK 500 15 LYS A 5 49.08 -84.26
REMARK 500 16 LYS A 5 49.32 -86.94
REMARK 500 18 LYS A 5 49.84 -81.81
REMARK 500 20 LYS A 5 49.45 -89.86
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1SFI RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF NATIVE SFTI-1
REMARK 900 RELATED ID: 1JBL RELATED DB: PDB
REMARK 900 NMR STRUCTURE OF NATIVE SFTI-1
REMARK 900 RELATED ID: 1JBN RELATED DB: PDB
REMARK 900 NMR STRUCTURE OF AN ACYCLIC PERMUTANT OF SFTI-1
REMARK 900 RELATED ID: 1O8Y RELATED DB: PDB
REMARK 900 NMR STRUCTURE OF AN ACYCLIC PERMUTANT OF SFTI-1
REMARK 900 RELATED ID: 1O8Z RELATED DB: PDB
REMARK 900 NMR STRUCTURE OF AN ACYCLIC PERMUTANT OF SFTI-1
DBREF 1T9E A 1 14 UNP Q4GWU5 SFTI1_HELAN 40 53
SEQADV 1T9E ABA A 3 UNP Q4GWU5 CYS 42 ENGINEERED MUTATION
SEQADV 1T9E ABA A 11 UNP Q4GWU5 CYS 50 ENGINEERED MUTATION
SEQRES 1 A 14 GLY ARG ABA THR LYS SER ILE PRO PRO ILE ABA PHE PRO
SEQRES 2 A 14 ASP
MODRES 1T9E ABA A 3 ALA ALPHA-AMINOBUTYRIC ACID
MODRES 1T9E ABA A 11 ALA ALPHA-AMINOBUTYRIC ACID
HET ABA A 3 13
HET ABA A 11 13
HETNAM ABA ALPHA-AMINOBUTYRIC ACID
FORMUL 1 ABA 2(C4 H9 N O2)
LINK C ARG A 2 N ABA A 3 1555 1555 1.32
LINK C ABA A 3 N THR A 4 1555 1555 1.33
LINK C ILE A 10 N ABA A 11 1555 1555 1.32
LINK C ABA A 11 N PHE A 12 1555 1555 1.32
LINK N GLY A 1 C ASP A 14 1555 1555 1.33
CISPEP 1 ILE A 7 PRO A 8 1 0.06
CISPEP 2 ILE A 7 PRO A 8 2 -0.02
CISPEP 3 ILE A 7 PRO A 8 3 -0.35
CISPEP 4 ILE A 7 PRO A 8 4 -0.26
CISPEP 5 ILE A 7 PRO A 8 5 -0.53
CISPEP 6 ILE A 7 PRO A 8 6 -0.39
CISPEP 7 ILE A 7 PRO A 8 7 -0.36
CISPEP 8 ILE A 7 PRO A 8 8 -0.25
CISPEP 9 ILE A 7 PRO A 8 9 -0.09
CISPEP 10 ILE A 7 PRO A 8 10 -0.46
CISPEP 11 ILE A 7 PRO A 8 11 -0.08
CISPEP 12 ILE A 7 PRO A 8 12 -0.17
CISPEP 13 ILE A 7 PRO A 8 13 -0.35
CISPEP 14 ILE A 7 PRO A 8 14 -0.13
CISPEP 15 ILE A 7 PRO A 8 15 -0.05
CISPEP 16 ILE A 7 PRO A 8 16 -0.39
CISPEP 17 ILE A 7 PRO A 8 17 -0.04
CISPEP 18 ILE A 7 PRO A 8 18 -0.11
CISPEP 19 ILE A 7 PRO A 8 19 -0.09
CISPEP 20 ILE A 7 PRO A 8 20 -0.22
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 - 25 20 Bytes