Header list of 2bi6.pdb file
Complete list - v 29 2 Bytes
HEADER CYSTEINE PROTEASE INHIBITOR 07-DEC-95 2BI6
TITLE NMR STUDY OF BROMELAIN INHIBITOR VI FROM PINEAPPLE STEM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BROMELAIN INHIBITOR VI;
COMPND 3 CHAIN: L;
COMPND 4 MOL_ID: 2;
COMPND 5 MOLECULE: BROMELAIN INHIBITOR VI;
COMPND 6 CHAIN: H
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ANANAS COMOSUS;
SOURCE 3 ORGANISM_COMMON: PINEAPPLE;
SOURCE 4 ORGANISM_TAXID: 4615;
SOURCE 5 TISSUE: STEM;
SOURCE 6 MOL_ID: 2;
SOURCE 7 ORGANISM_SCIENTIFIC: ANANAS COMOSUS;
SOURCE 8 ORGANISM_COMMON: PINEAPPLE;
SOURCE 9 ORGANISM_TAXID: 4615;
SOURCE 10 TISSUE: STEM
KEYWDS CYSTEINE PROTEASE INHIBITOR
EXPDTA SOLUTION NMR
NUMMDL 18
AUTHOR K.-I.HATANO
REVDAT 4 29-NOV-17 2BI6 1 REMARK HELIX
REVDAT 3 24-FEB-09 2BI6 1 VERSN
REVDAT 2 01-APR-03 2BI6 1 JRNL
REVDAT 1 03-APR-96 2BI6 0
JRNL AUTH K.HATANO,M.KOJIMA,M.TANOKURA,K.TAKAHASHI
JRNL TITL SOLUTION STRUCTURE OF BROMELAIN INHIBITOR IV FROM PINEAPPLE
JRNL TITL 2 STEM: STRUCTURAL SIMILARITY WITH BOWMAN-BIRK
JRNL TITL 3 TRYPSIN/CHYMOTRYPSIN INHIBITOR FROM SOYBEAN.
JRNL REF BIOCHEMISTRY V. 35 5379 1996
JRNL REFN ISSN 0006-2960
JRNL PMID 8611527
JRNL DOI 10.1021/BI952754+
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH K.HATANO,M.KOJIMA,M.TANOKURA,K.TAKAHASHI
REMARK 1 TITL PRIMARY STRUCTURE,SEQUENCE-SPECIFIC 1H ASSIGNMENTS AND
REMARK 1 TITL 2 SECONDARY STRUCTURE IN SOLUTION OF BROMELAIN INHIBITOR VI
REMARK 1 TITL 3 FROM PINEAPPLE STEM
REMARK 1 REF EUR.J.BIOCHEM. V. 232 335 1995
REMARK 1 REFN ISSN 0014-2956
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2BI6 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_1000177831.
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 : 18
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, H
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 ALA L 2 179.38 -53.63
REMARK 500 1 GLU L 5 71.70 -104.11
REMARK 500 1 CYS L 8 52.23 -150.99
REMARK 500 1 LEU L 10 105.60 73.07
REMARK 500 1 GLU H 2 53.23 -146.38
REMARK 500 1 TYR H 3 -177.85 175.62
REMARK 500 1 CYS H 5 157.96 68.49
REMARK 500 1 PHE H 25 17.41 49.76
REMARK 500 1 SER H 35 95.51 -163.18
REMARK 500 1 ASN H 37 -51.70 -139.12
REMARK 500 1 ASP H 38 -55.86 163.98
REMARK 500 1 CYS H 39 149.89 -171.33
REMARK 500 1 VAL H 40 39.38 -92.12
REMARK 500 2 CYS L 8 61.74 -150.05
REMARK 500 2 LEU L 10 53.68 178.10
REMARK 500 2 GLU H 2 156.86 174.90
REMARK 500 2 TYR H 3 -90.23 -55.51
REMARK 500 2 LYS H 4 63.83 6.14
REMARK 500 2 THR H 8 31.54 -144.28
REMARK 500 2 ASP H 13 137.38 176.41
REMARK 500 2 THR H 20 78.50 -112.89
REMARK 500 2 CYS H 21 -169.80 -115.73
REMARK 500 2 PHE H 25 15.87 49.99
REMARK 500 2 LEU H 31 23.77 -159.09
REMARK 500 2 SER H 35 78.02 179.31
REMARK 500 2 ASN H 37 -176.83 -170.60
REMARK 500 2 VAL H 40 39.81 -89.49
REMARK 500 3 ALA L 2 -154.11 -75.47
REMARK 500 3 GLU L 5 59.46 -104.21
REMARK 500 3 LEU L 10 61.43 -106.97
REMARK 500 3 TYR H 3 -177.82 46.65
REMARK 500 3 CYS H 5 155.98 83.14
REMARK 500 3 THR H 20 45.70 -160.41
REMARK 500 3 PHE H 25 -60.05 -11.61
REMARK 500 3 LEU H 31 30.55 -141.32
REMARK 500 3 ILE H 34 -73.98 -170.20
REMARK 500 3 SER H 35 99.76 52.62
REMARK 500 3 VAL H 40 -132.28 -110.90
REMARK 500 4 GLU L 5 87.48 -69.79
REMARK 500 4 CYS L 8 65.94 -161.44
REMARK 500 4 LEU L 10 92.12 -49.53
REMARK 500 4 GLU H 2 159.00 -49.39
REMARK 500 4 TYR H 3 -151.31 36.68
REMARK 500 4 LYS H 4 -90.43 -97.69
REMARK 500 4 CYS H 5 157.10 178.25
REMARK 500 4 THR H 8 32.87 -142.53
REMARK 500 4 ASP H 13 143.41 -174.19
REMARK 500 4 THR H 20 79.13 -102.17
REMARK 500 4 CYS H 21 -159.53 -128.28
REMARK 500 4 PHE H 25 19.52 49.98
REMARK 500
REMARK 500 THIS ENTRY HAS 227 RAMACHANDRAN OUTLIERS.
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 L 11 0.27 SIDE CHAIN
REMARK 500 2 ARG L 11 0.09 SIDE CHAIN
REMARK 500 3 ARG L 11 0.19 SIDE CHAIN
REMARK 500 4 ARG L 11 0.32 SIDE CHAIN
REMARK 500 5 ARG L 11 0.30 SIDE CHAIN
REMARK 500 6 ARG L 11 0.32 SIDE CHAIN
REMARK 500 7 ARG L 11 0.12 SIDE CHAIN
REMARK 500 8 ARG L 11 0.24 SIDE CHAIN
REMARK 500 9 ARG L 11 0.32 SIDE CHAIN
REMARK 500 10 ARG L 11 0.21 SIDE CHAIN
REMARK 500 11 ARG L 11 0.17 SIDE CHAIN
REMARK 500 12 ARG L 11 0.30 SIDE CHAIN
REMARK 500 13 ARG L 11 0.32 SIDE CHAIN
REMARK 500 14 ARG L 11 0.19 SIDE CHAIN
REMARK 500 15 ARG L 11 0.29 SIDE CHAIN
REMARK 500 16 ARG L 11 0.26 SIDE CHAIN
REMARK 500 17 ARG L 11 0.32 SIDE CHAIN
REMARK 500 18 ARG L 11 0.21 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: B1
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1BI6 RELATED DB: PDB
DBREF 2BI6 L 1 11 UNP P27478 IBR2_ANACO 1 11
DBREF 2BI6 H 1 41 UNP P27478 IBR2_ANACO 12 52
SEQRES 1 L 11 THR ALA CYS SER GLU CYS VAL CYS PRO LEU ARG
SEQRES 1 H 41 GLU GLU TYR LYS CYS TYR CYS THR ASP THR TYR SER ASP
SEQRES 2 H 41 CYS PRO GLY PHE CYS LYS THR CYS LYS ALA GLU PHE GLY
SEQRES 3 H 41 LYS TYR ILE CYS LEU ASP LEU ILE SER PRO ASN ASP CYS
SEQRES 4 H 41 VAL LYS
SHEET 1 B1 3 LYS H 22 GLU H 24 0
SHEET 2 B1 3 LYS H 27 ILE H 29 -1 N ILE H 29 O LYS H 22
SHEET 3 B1 3 ASP H 9 TYR H 11 1 N TYR H 11 O TYR H 28
SHEET 1 B2 3 ASP H 32 ILE H 34 0
SHEET 2 B2 3 CYS H 5 CYS H 7 -1 O CYS H 7 N ASP H 32
SHEET 3 B2 3 CYS L 6 CYS L 8 1 N VAL L 7 O TYR H 6
SSBOND 1 CYS L 3 CYS H 7 1555 1555 2.02
SSBOND 2 CYS L 6 CYS H 39 1555 1555 2.02
SSBOND 3 CYS L 8 CYS H 5 1555 1555 2.02
SSBOND 4 CYS H 14 CYS H 21 1555 1555 2.02
SSBOND 5 CYS H 18 CYS H 30 1555 1555 2.02
SITE 1 B1 2 LEU L 10 ARG L 11
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 - v 29 2 Bytes