Header list of 1ib9.pdb file
Complete list - 23 20 Bytes
HEADER PLANT PROTEIN 28-MAR-01 1IB9
TITLE SOLUTION STRUCTURE OF MCOTI-II, A MACROCYCLIC TRYPSIN INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRYPSIN INHIBITOR II;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: MCOTI-II
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MOMORDICA COCHINCHINENSIS;
SOURCE 3 ORGANISM_COMMON: SPINY BITTER CUCUMBER;
SOURCE 4 ORGANISM_TAXID: 3674;
SOURCE 5 OTHER_DETAILS: THE PROTEIN IS ISOLATED FROM THE SEEDS USING SODIUM
SOURCE 6 ACETATE.
KEYWDS CYCLIC CYSTINE KNOT, CYCLOTIDE, CIRCULAR PROTEIN, BETA-HAIRPIN, PLANT
KEYWDS 2 PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR M.E.FELIZMENIO-QUIMIO,N.L.DALY,D.J.CRAIK
REVDAT 4 23-FEB-22 1IB9 1 REMARK
REVDAT 3 24-FEB-09 1IB9 1 VERSN
REVDAT 2 01-APR-03 1IB9 1 JRNL
REVDAT 1 18-JUL-01 1IB9 0
JRNL AUTH M.E.FELIZMENIO-QUIMIO,N.L.DALY,D.J.CRAIK
JRNL TITL CIRCULAR PROTEINS IN PLANTS: SOLUTION STRUCTURE OF A NOVEL
JRNL TITL 2 MACROCYCLIC TRYPSIN INHIBITOR FROM MOMORDICA
JRNL TITL 3 COCHINCHINENSIS.
JRNL REF J.BIOL.CHEM. V. 276 22875 2001
JRNL REFN ISSN 0021-9258
JRNL PMID 11292835
JRNL DOI 10.1074/JBC.M101666200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, X-PLOR 3.851
REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 420 RESTRAINTS, 383 ARE NOE-
REMARK 3 DERIVED,
REMARK 3 25 DIHEDRAL ANGLE RESTRAINTS AND 12 FROM HYDROGEN BONDS.
REMARK 4
REMARK 4 1IB9 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-MAR-01.
REMARK 100 THE DEPOSITION ID IS D_1000013122.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 3.5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1 MM MCOTI-II, 90% H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; DQF-COSY; E-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XEASY 1.3.7, DYANA 1.5, X-PLOR
REMARK 210 3.851
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : THE SUBMITTED CONFORMER MODELS
REMARK 210 ARE THOSE WITH THE FEWEST NUMBER
REMARK 210 OF RESTRAINT VIOLATIONS.
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 17
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 400
REMARK 400 COMPOUND
REMARK 400
REMARK 400 THE CYCLIC KNOTTIN TRYPSIN INHIBITOR II IS CYCLIC PEPTIDE, A MEMBER
REMARK 400 OF ANTIMICROBIAL, ANTITUMOR CLASS.
REMARK 400
REMARK 400 GROUP: 1
REMARK 400 NAME: CYCLIC KNOTTIN TRYPSIN INHIBITOR II
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 N SER A 1 C GLY A 34 1.31
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 CYS A 33 CA - CB - SG ANGL. DEV. = 8.8 DEGREES
REMARK 500 2 CYS A 33 CA - CB - SG ANGL. DEV. = 10.6 DEGREES
REMARK 500 3 CYS A 33 CA - CB - SG ANGL. DEV. = 8.1 DEGREES
REMARK 500 4 CYS A 33 CA - CB - SG ANGL. DEV. = 8.7 DEGREES
REMARK 500 5 CYS A 33 CA - CB - SG ANGL. DEV. = 8.5 DEGREES
REMARK 500 6 CYS A 33 CA - CB - SG ANGL. DEV. = 9.7 DEGREES
REMARK 500 7 CYS A 33 CA - CB - SG ANGL. DEV. = 8.4 DEGREES
REMARK 500 8 CYS A 33 CA - CB - SG ANGL. DEV. = 10.6 DEGREES
REMARK 500 9 CYS A 33 CA - CB - SG ANGL. DEV. = 8.6 DEGREES
REMARK 500 10 CYS A 33 CA - CB - SG ANGL. DEV. = 10.8 DEGREES
REMARK 500 11 CYS A 33 CA - CB - SG ANGL. DEV. = 11.4 DEGREES
REMARK 500 12 CYS A 33 CA - CB - SG ANGL. DEV. = 9.8 DEGREES
REMARK 500 13 CYS A 33 CA - CB - SG ANGL. DEV. = 10.7 DEGREES
REMARK 500 14 CYS A 33 CA - CB - SG ANGL. DEV. = 8.9 DEGREES
REMARK 500 15 CYS A 33 CA - CB - SG ANGL. DEV. = 10.2 DEGREES
REMARK 500 16 CYS A 33 CA - CB - SG ANGL. DEV. = 9.3 DEGREES
REMARK 500 17 CYS A 33 CA - CB - SG ANGL. DEV. = 10.7 DEGREES
REMARK 500 18 CYS A 33 CA - CB - SG ANGL. DEV. = 8.6 DEGREES
REMARK 500 19 CYS A 33 CA - CB - SG ANGL. DEV. = 10.5 DEGREES
REMARK 500 20 CYS A 33 CA - CB - SG ANGL. DEV. = 9.2 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 PRO A 9 -159.81 -70.48
REMARK 500 1 LEU A 12 24.26 -162.64
REMARK 500 1 CYS A 33 159.81 -40.69
REMARK 500 2 LYS A 10 108.14 -59.04
REMARK 500 2 LEU A 12 41.56 -107.27
REMARK 500 3 LEU A 12 36.78 -87.19
REMARK 500 3 CYS A 33 164.91 -37.71
REMARK 500 4 PRO A 9 -167.89 -68.98
REMARK 500 4 LEU A 12 46.02 -94.84
REMARK 500 4 CYS A 33 155.39 -37.31
REMARK 500 5 SER A 3 -136.00 -150.25
REMARK 500 5 PRO A 9 102.24 -54.62
REMARK 500 5 LYS A 10 83.12 -63.65
REMARK 500 5 ILE A 26 -168.54 -122.91
REMARK 500 5 CYS A 33 154.73 -40.93
REMARK 500 6 ASP A 4 -22.88 69.33
REMARK 500 6 PRO A 9 -161.12 -65.01
REMARK 500 6 LEU A 12 21.25 -173.79
REMARK 500 6 CYS A 33 153.23 -41.14
REMARK 500 7 SER A 3 -133.33 -89.91
REMARK 500 7 LEU A 12 38.32 -89.83
REMARK 500 7 CYS A 33 153.44 -39.95
REMARK 500 8 PRO A 9 87.35 -56.45
REMARK 500 8 LEU A 12 39.77 -86.13
REMARK 500 8 CYS A 33 150.10 -46.10
REMARK 500 9 SER A 3 -48.83 -150.29
REMARK 500 9 ILE A 26 -159.99 -131.04
REMARK 500 9 CYS A 33 158.10 -40.62
REMARK 500 10 SER A 3 -16.67 -142.32
REMARK 500 10 VAL A 7 44.12 -92.16
REMARK 500 10 LEU A 12 49.60 -104.96
REMARK 500 10 CYS A 33 161.15 -46.78
REMARK 500 11 SER A 19 32.52 -86.75
REMARK 500 11 CYS A 33 153.89 -48.43
REMARK 500 12 SER A 3 -152.76 -150.56
REMARK 500 12 VAL A 7 37.86 -90.06
REMARK 500 12 PRO A 9 -157.81 -64.35
REMARK 500 12 LYS A 10 33.00 -143.18
REMARK 500 12 SER A 19 20.88 -79.62
REMARK 500 12 CYS A 33 157.24 -47.60
REMARK 500 13 SER A 3 -148.02 -89.78
REMARK 500 13 PRO A 9 95.41 -64.20
REMARK 500 13 LEU A 12 81.96 -67.30
REMARK 500 13 CYS A 33 154.35 -44.49
REMARK 500 14 CYS A 33 152.29 -41.22
REMARK 500 15 LYS A 14 144.40 -36.32
REMARK 500 15 ARG A 16 -63.46 -91.48
REMARK 500 15 ARG A 28 170.04 -59.08
REMARK 500 16 PRO A 9 28.03 -79.67
REMARK 500 16 LEU A 12 70.25 -62.96
REMARK 500
REMARK 500 THIS ENTRY HAS 64 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 CYS A 8 PRO A 9 8 142.11
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1IB9 A 1 34 UNP P82409 ITR2_MOMCO 1 34
SEQRES 1 A 34 SER GLY SER ASP GLY GLY VAL CYS PRO LYS ILE LEU LYS
SEQRES 2 A 34 LYS CYS ARG ARG ASP SER ASP CYS PRO GLY ALA CYS ILE
SEQRES 3 A 34 CYS ARG GLY ASN GLY TYR CYS GLY
HELIX 1 1 ARG A 17 CYS A 21 5 5
SHEET 1 A 2 ILE A 26 CYS A 27 0
SHEET 2 A 2 CYS A 33 GLY A 34 -1 N GLY A 34 O ILE A 26
SSBOND 1 CYS A 8 CYS A 25 1555 1555 2.02
SSBOND 2 CYS A 15 CYS A 27 1555 1555 2.02
SSBOND 3 CYS A 21 CYS A 33 1555 1555 2.01
CRYST1 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