Header list of 1eqk.pdb file
Complete list - b 16 2 Bytes
HEADER HYDROLASE INHIBITOR 05-APR-00 1EQK
TITLE SOLUTION STRUCTURE OF ORYZACYSTATIN-I, A CYSTEINE PROTEINASE INHIBITOR
TITLE 2 OF THE RICE, ORYZA SATIVA L. JAPONICA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ORYZACYSTATIN-I;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ORYZA SATIVA JAPONICA GROUP;
SOURCE 3 ORGANISM_TAXID: 39947;
SOURCE 4 STRAIN: JAPONICA GROUP;
SOURCE 5 TISSUE: SEED;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PLASMID PET-26B(+)
KEYWDS ALPHA AND BETA PROTEINS, CYSTATIN-LIKE FOLD, CYSTATIN/MONELLIN
KEYWDS 2 SUPERFAMILY, PHYTOCYSTATIN FAMILY, HYDROLASE INHIBITOR
EXPDTA SOLUTION NMR
NUMMDL 21
MDLTYP MINIMIZED AVERAGE
AUTHOR K.NAGATA,N.KUDO,K.ABE,S.ARAI,M.TANOKURA
REVDAT 3 16-FEB-22 1EQK 1 REMARK
REVDAT 2 24-FEB-09 1EQK 1 VERSN
REVDAT 1 10-JAN-01 1EQK 0
JRNL AUTH K.NAGATA,N.KUDO,K.ABE,S.ARAI,M.TANOKURA
JRNL TITL THREE-DIMENSIONAL SOLUTION STRUCTURE OF ORYZACYSTATIN-I, A
JRNL TITL 2 CYSTEINE PROTEINASE INHIBITOR OF THE RICE, ORYZA SATIVA L.
JRNL TITL 3 JAPONICA.
JRNL REF BIOCHEMISTRY V. 39 14753 2000
JRNL REFN ISSN 0006-2960
JRNL PMID 11101290
JRNL DOI 10.1021/BI0006971
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 5.3B, CNS 0.9
REMARK 3 AUTHORS : VARIAN (VNMR),
REMARK 3 BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-KUNSTLEVE,JIANG,KUSZEWSKI,
REMARK 3 NILGES,PANNU,READ,RICE,SIMONSON,WARREN (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: A TOTAL OF 1383 RESTRAINTS, CONSISTING
REMARK 3 OF 1183 INTERPROTON DISTANCE RESTRAINTS (338 LONG-RANGE (|I - J|
REMARK 3 >= 6), 228 MEDIUM-RANGE (2 <= |I - J| <= 5), 351 SEQUENTIAL (|I -
REMARK 3 J| = 1) AND 266 INTRARESIDUAL (|I - J| = 0)), 108 HYDROGEN BOND
REMARK 3 RESTRAINTS (REPRESENTING 54 HYDROGEN BONDS) AND 92 TORSION ANGLE
REMARK 3 RESTRAINTS (54 PHI AND 38 CHI1), WERE USED IN THE STRUCTURE
REMARK 3 CALCULATIONS BY TORSION ANGLE DYNAMICS USING DYANA (VER. 1.4). A
REMARK 3 FINAL SET OF 20 STRUCTURES WAS SELECTED FROM 100 CALCULATIONS ON
REMARK 3 THE BASIS OF AGREEMENT WITH THE EXPERIMENTAL DATA AND VAN DER
REMARK 3 WAALS' ENERGY. THE AVERAGE COORDINATES OF THE 20 DYANA
REMARK 3 STRUCTURES WERE SUBJECTED TO ENERGY-MINIMIZATION USING CNS (VER.
REMARK 3 0.9).
REMARK 4
REMARK 4 1EQK COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-APR-00.
REMARK 100 THE DEPOSITION ID IS D_1000010822.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.8
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 3 MM ORYZACYSTATIN-I; 50 MM
REMARK 210 SODIUM PHOSPHATE/100 MM NACL/
REMARK 210 0.02% NAN3, PH 6.8; 10% D2O/90%
REMARK 210 H2O; 2 MM ORYZACYSTATIN-I U-15N;
REMARK 210 50 MM SODIUM PHOSPHATE/100 MM
REMARK 210 NACL/0.02% NAN3, PH 6.8; 10% D2O/
REMARK 210 90% H2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; HNHA
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 1.6, NMRDRAW 1.6, FELIX
REMARK 210 95, PIPP/CAPP 4.0, DYANA 1.4,
REMARK 210 AQUA 2.0, PROCHECK-NMR 3.4,
REMARK 210 MOLMOL 2.6
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 21
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH FAVORABLE NON
REMARK 210 -BOND ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 21
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING 1H AND 15N NMR
REMARK 210 SPECTROSCOPY.
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
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 SER A 2 107.02 179.46
REMARK 500 1 SER A 3 131.76 -175.26
REMARK 500 1 ASP A 4 112.93 -174.87
REMARK 500 1 LEU A 9 3.89 -155.99
REMARK 500 1 VAL A 12 75.77 38.00
REMARK 500 1 ASN A 17 84.12 51.51
REMARK 500 1 GLU A 18 -17.88 -46.19
REMARK 500 1 THR A 32 -70.22 -61.29
REMARK 500 1 SER A 40 154.87 75.73
REMARK 500 1 LEU A 41 -43.15 -159.31
REMARK 500 1 LYS A 46 -170.21 -179.20
REMARK 500 1 VAL A 55 -118.34 -156.11
REMARK 500 1 TRP A 84 -19.14 -46.68
REMARK 500 1 MET A 85 14.71 -142.45
REMARK 500 1 ASP A 86 81.57 37.35
REMARK 500 1 GLU A 92 136.01 164.84
REMARK 500 1 VAL A 96 83.88 50.18
REMARK 500 1 ASN A 101 130.09 179.17
REMARK 500 2 VAL A 15 -165.38 -126.33
REMARK 500 2 ASN A 17 101.61 173.48
REMARK 500 2 THR A 32 -70.23 -70.83
REMARK 500 2 ASN A 39 25.78 43.35
REMARK 500 2 SER A 40 153.37 74.22
REMARK 500 2 LEU A 41 -15.21 -160.08
REMARK 500 2 LYS A 46 -175.98 -177.22
REMARK 500 2 VAL A 55 -118.98 -155.63
REMARK 500 2 TRP A 84 -14.98 -46.45
REMARK 500 2 MET A 85 10.35 -146.93
REMARK 500 2 ASP A 86 83.03 42.53
REMARK 500 2 LYS A 88 149.27 -178.44
REMARK 500 2 GLU A 89 115.09 -161.78
REMARK 500 2 GLU A 92 135.51 164.31
REMARK 500 2 VAL A 96 88.92 55.50
REMARK 500 2 ALA A 98 -29.74 -171.73
REMARK 500 2 SER A 99 -172.44 62.52
REMARK 500 2 ALA A 100 -80.16 75.47
REMARK 500 2 ASN A 101 -54.85 -149.11
REMARK 500 3 SER A 2 25.76 -143.07
REMARK 500 3 ASN A 17 82.96 60.00
REMARK 500 3 THR A 32 -72.08 -70.92
REMARK 500 3 SER A 40 150.63 75.31
REMARK 500 3 LEU A 41 -39.85 -151.36
REMARK 500 3 LEU A 42 -155.34 -162.78
REMARK 500 3 LYS A 46 -168.13 -178.47
REMARK 500 3 SER A 49 -169.13 -161.31
REMARK 500 3 VAL A 55 -119.45 -154.58
REMARK 500 3 TRP A 84 -15.14 -46.72
REMARK 500 3 ASP A 86 82.64 43.63
REMARK 500 3 GLU A 92 164.98 170.06
REMARK 500 3 PHE A 93 96.90 -161.98
REMARK 500
REMARK 500 THIS ENTRY HAS 379 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1EQK A 1 102 UNP P09229 CYT1_ORYSA 1 102
SEQRES 1 A 102 MET SER SER ASP GLY GLY PRO VAL LEU GLY GLY VAL GLU
SEQRES 2 A 102 PRO VAL GLY ASN GLU ASN ASP LEU HIS LEU VAL ASP LEU
SEQRES 3 A 102 ALA ARG PHE ALA VAL THR GLU HIS ASN LYS LYS ALA ASN
SEQRES 4 A 102 SER LEU LEU GLU PHE GLU LYS LEU VAL SER VAL LYS GLN
SEQRES 5 A 102 GLN VAL VAL ALA GLY THR LEU TYR TYR PHE THR ILE GLU
SEQRES 6 A 102 VAL LYS GLU GLY ASP ALA LYS LYS LEU TYR GLU ALA LYS
SEQRES 7 A 102 VAL TRP GLU LYS PRO TRP MET ASP PHE LYS GLU LEU GLN
SEQRES 8 A 102 GLU PHE LYS PRO VAL ASP ALA SER ALA ASN ALA
HELIX 1 1 ASP A 20 ALA A 38 1 19
SHEET 1 A 5 GLU A 13 VAL A 15 0
SHEET 2 A 5 LEU A 42 VAL A 54 -1 N VAL A 50 O VAL A 15
SHEET 3 A 5 THR A 58 GLU A 68 -1 O LEU A 59 N GLN A 53
SHEET 4 A 5 LYS A 73 GLU A 81 -1 N LYS A 73 O VAL A 66
SHEET 5 A 5 LEU A 90 LYS A 94 -1 N GLN A 91 O LYS A 78
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 - b 16 2 Bytes