Header list of 1nb1.pdb file
Complete list - 23 20 Bytes
HEADER ANTIBIOTIC 01-DEC-02 1NB1
TITLE HIGH RESOLUTION SOLUTION STRUCTURE OF KALATA B1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: KALATA B1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 1-29
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: OLDENLANDIA AFFINIS;
SOURCE 3 ORGANISM_TAXID: 60225
KEYWDS CYCLOTIDE, CYCLIC BACKBONE, CYSTINE KNOT, CCK, INSECTICIDAL,
KEYWDS 2 ANTIBIOTIC
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR K.J.ROSENGREN,N.L.DALY,M.R.PLAN,C.WAINE,D.J.CRAIK
REVDAT 4 23-FEB-22 1NB1 1 REMARK
REVDAT 3 24-FEB-09 1NB1 1 VERSN
REVDAT 2 08-MAR-05 1NB1 1 REMARK
REVDAT 1 18-MAR-03 1NB1 0
JRNL AUTH K.J.ROSENGREN,N.L.DALY,M.R.PLAN,C.WAINE,D.J.CRAIK
JRNL TITL TWISTS, KNOTS, AND RINGS IN PROTEINS. STRUCTURAL DEFINITION
JRNL TITL 2 OF THE CYCLOTIDE FRAMEWORK
JRNL REF J.BIOL.CHEM. V. 278 8606 2003
JRNL REFN ISSN 0021-9258
JRNL PMID 12482868
JRNL DOI 10.1074/JBC.M211147200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, CNS 1.0
REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER A.T., ADAMS P.D., CLORE
REMARK 3 G.M., DELANO W.L., GROS P., GROSSE-KUNSTLEVE R.W.,
REMARK 3 JIANG J.S., KUSZEWSKI J., NILGES M., PANNU N.S.,
REMARK 3 READ R.J., RICE L.M., SIMONSON T. AND WARREN G.L.
REMARK 3 (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1NB1 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 05-DEC-02.
REMARK 100 THE DEPOSITION ID IS D_1000017729.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.1
REMARK 210 IONIC STRENGTH : 0
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 5MM OF PEPTIDE IN 0.5ML; 5MM OF
REMARK 210 PEPTIDE IN 0.5ML
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : DQF-COSY; 2D TOCSY; 2D NOESY; E
REMARK 210 -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 : XEASY 1.3.7, DYANA 1.5
REMARK 210 METHOD USED : STRUCTURES WERE CALCULATED USING
REMARK 210 TORSION ANGLE DYNAMICS AND
REMARK 210 REFINED IN EXPLICIT SOLVENT
REMARK 210 USING CARTESIAN DYNAMICS AND
REMARK 210 POWELL RESTRAINED MINIMISATION.
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 : 1
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D NMR
REMARK 210 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: 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 N CYS A 1 C VAL A 29 1.32
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 TRP A 19 129.64 -28.72
REMARK 500 2 TRP A 19 129.37 -28.07
REMARK 500 3 TRP A 19 129.32 -27.99
REMARK 500 4 TRP A 19 129.54 -28.54
REMARK 500 5 TRP A 19 129.98 -28.65
REMARK 500 6 TRP A 19 129.57 -28.36
REMARK 500 7 TRP A 19 129.68 -28.53
REMARK 500 8 TRP A 19 129.57 -28.29
REMARK 500 9 TRP A 19 129.64 -27.94
REMARK 500 9 ASN A 25 29.92 48.03
REMARK 500 10 TRP A 19 129.60 -28.02
REMARK 500 10 PRO A 28 105.88 -58.07
REMARK 500 11 TRP A 19 129.48 -28.45
REMARK 500 11 PRO A 28 105.91 -59.22
REMARK 500 12 TRP A 19 129.45 -28.21
REMARK 500 13 TRP A 19 129.45 -28.11
REMARK 500 14 TRP A 19 129.65 -28.32
REMARK 500 15 TRP A 19 129.39 -27.94
REMARK 500 16 TRP A 19 129.60 -28.14
REMARK 500 16 ASN A 25 28.83 49.36
REMARK 500 17 TRP A 19 129.44 -28.16
REMARK 500 18 TRP A 19 129.53 -28.24
REMARK 500 19 TRP A 19 129.52 -28.30
REMARK 500 20 TRP A 19 129.26 -27.73
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1KAL RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF KALATA B1
DBREF 1NB1 A 1 28 UNP P56254 KAB1_OLDAF 93 120
SEQRES 1 A 29 CYS GLY GLU THR CYS VAL GLY GLY THR CYS ASN THR PRO
SEQRES 2 A 29 GLY CYS THR CYS SER TRP PRO VAL CYS THR ARG ASN GLY
SEQRES 3 A 29 LEU PRO VAL
SHEET 1 A 2 CYS A 15 SER A 18 0
SHEET 2 A 2 VAL A 21 ARG A 24 -1 O THR A 23 N THR A 16
SSBOND 1 CYS A 1 CYS A 15 1555 1555 2.02
SSBOND 2 CYS A 5 CYS A 17 1555 1555 2.04
SSBOND 3 CYS A 10 CYS A 22 1555 1555 2.03
CISPEP 1 TRP A 19 PRO A 20 1 0.39
CISPEP 2 TRP A 19 PRO A 20 2 0.27
CISPEP 3 TRP A 19 PRO A 20 3 0.32
CISPEP 4 TRP A 19 PRO A 20 4 0.42
CISPEP 5 TRP A 19 PRO A 20 5 0.30
CISPEP 6 TRP A 19 PRO A 20 6 0.32
CISPEP 7 TRP A 19 PRO A 20 7 0.36
CISPEP 8 TRP A 19 PRO A 20 8 0.38
CISPEP 9 TRP A 19 PRO A 20 9 0.32
CISPEP 10 TRP A 19 PRO A 20 10 0.36
CISPEP 11 TRP A 19 PRO A 20 11 0.42
CISPEP 12 TRP A 19 PRO A 20 12 0.36
CISPEP 13 TRP A 19 PRO A 20 13 0.32
CISPEP 14 TRP A 19 PRO A 20 14 0.31
CISPEP 15 TRP A 19 PRO A 20 15 0.47
CISPEP 16 TRP A 19 PRO A 20 16 0.31
CISPEP 17 TRP A 19 PRO A 20 17 0.33
CISPEP 18 TRP A 19 PRO A 20 18 0.43
CISPEP 19 TRP A 19 PRO A 20 19 0.34
CISPEP 20 TRP A 19 PRO A 20 20 0.37
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 - 23 20 Bytes