Header list of 1iy5.pdb file
Complete list - 23 20 Bytes
HEADER HYDROLASE 23-JUL-02 1IY5
TITLE SOLUTION STRUCTURE OF WILD TYPE OMSVP3
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: OMSVP3;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: THIRD DOMAIN;
COMPND 5 SYNONYM: OVOMUCOID;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LOPHURA NYCTHEMERA;
SOURCE 3 ORGANISM_COMMON: SILVER PHEASANT;
SOURCE 4 ORGANISM_TAXID: 9046;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET22B
KEYWDS SOLUTION STRUCTURE, CSH MOTIF, OMSVP3, OVOMUCOID THIRD DOMAIN,
KEYWDS 2 PROTEASE INHIBITOR, HYDROLASE
EXPDTA SOLUTION NMR
NUMMDL 15
AUTHOR H.HEMMI,T.KUMAZAKI,T.YAMAZAKI,S.KOJIMA,T.YOSHIDA,Y.KYOGOKU,M.KATSU,
AUTHOR 2 H.YOKOSAWA,K.MIURA,Y.KOBAYASHI
REVDAT 3 23-FEB-22 1IY5 1 REMARK
REVDAT 2 24-FEB-09 1IY5 1 VERSN
REVDAT 1 11-MAR-03 1IY5 0
JRNL AUTH H.HEMMI,T.KUMAZAKI,T.YAMAZAKI,S.KOJIMA,T.YOSHIDA,Y.KYOGOKU,
JRNL AUTH 2 M.KATSU,F.SHINOHARA,H.YOKOSAWA,K.MIURA,Y.KOBAYASHI
JRNL TITL INHIBITORY SPECIFICITY CHANGE OF OVOMUCOID THIRD DOMAIN OF
JRNL TITL 2 THE SILVER PHEASANT UPON INTRODUCTION OF AN ENGINEERED
JRNL TITL 3 CYS14-CYS39 BOND
JRNL REF BIOCHEMISTRY V. 42 2524 2003
JRNL REFN ISSN 0006-2960
JRNL PMID 12614146
JRNL DOI 10.1021/BI026727C
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, X-PLOR 3.1
REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1IY5 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-JUL-02.
REMARK 100 THE DEPOSITION ID IS D_1000005395.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 4.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 4.0MM OMSVP3; 90%H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; DQF-COSY; TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : AMX; DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 2.1, NMRPIPP 4.3.2
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOW TOTAL ENERGY AND LOW
REMARK 210 DEVIATION FROM MEAN STRUCTURE
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 11
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 VAL A 6 164.80 55.72
REMARK 500 1 CYS A 8 55.04 -102.25
REMARK 500 1 ALA A 15 146.89 169.06
REMARK 500 1 TYR A 20 45.72 -97.66
REMARK 500 1 ASN A 33 173.88 177.71
REMARK 500 1 THR A 49 -165.04 -120.36
REMARK 500 1 HIS A 52 108.33 178.98
REMARK 500 1 PHE A 53 92.48 -43.63
REMARK 500 2 SER A 5 -57.16 161.20
REMARK 500 2 CYS A 8 53.35 -99.67
REMARK 500 2 GLU A 10 44.34 -89.33
REMARK 500 2 ASN A 33 -165.32 176.37
REMARK 500 2 THR A 49 -149.98 -132.20
REMARK 500 2 HIS A 52 104.84 177.61
REMARK 500 2 PHE A 53 93.83 -44.84
REMARK 500 3 ASP A 7 86.48 -69.50
REMARK 500 3 CYS A 8 31.75 -89.15
REMARK 500 3 GLU A 10 35.00 -90.87
REMARK 500 3 GLU A 19 173.07 -54.95
REMARK 500 3 TYR A 20 37.18 -140.80
REMARK 500 3 ASN A 33 172.09 172.87
REMARK 500 3 THR A 49 -152.03 -123.85
REMARK 500 3 HIS A 52 110.07 176.99
REMARK 500 3 PHE A 53 93.72 -42.27
REMARK 500 4 VAL A 4 -48.53 -137.41
REMARK 500 4 SER A 5 -58.25 175.57
REMARK 500 4 ASN A 33 169.77 173.71
REMARK 500 4 ASN A 45 -0.47 75.51
REMARK 500 4 THR A 47 42.48 -101.46
REMARK 500 4 THR A 49 -157.09 -109.60
REMARK 500 4 HIS A 52 105.15 167.55
REMARK 500 4 PHE A 53 99.88 -47.00
REMARK 500 5 SER A 5 -91.70 49.46
REMARK 500 5 CYS A 8 45.17 -81.90
REMARK 500 5 ALA A 15 144.11 -176.62
REMARK 500 5 CYS A 16 -166.54 -126.31
REMARK 500 5 SER A 26 -18.17 -48.84
REMARK 500 5 ASN A 33 -172.47 175.09
REMARK 500 5 ASN A 45 -0.47 76.90
REMARK 500 5 THR A 49 -153.55 -137.75
REMARK 500 5 HIS A 52 109.55 178.09
REMARK 500 5 PHE A 53 103.67 -44.60
REMARK 500 6 CYS A 8 40.44 -80.66
REMARK 500 6 ALA A 15 -171.36 168.58
REMARK 500 6 ASN A 33 -168.17 172.84
REMARK 500 6 THR A 49 -152.63 -98.22
REMARK 500 6 HIS A 52 111.62 177.73
REMARK 500 6 PHE A 53 93.86 -43.35
REMARK 500 7 SER A 5 -56.48 83.97
REMARK 500 7 CYS A 16 -164.39 -116.44
REMARK 500
REMARK 500 THIS ENTRY HAS 116 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 A 21 0.32 SIDE CHAIN
REMARK 500 2 ARG A 21 0.16 SIDE CHAIN
REMARK 500 3 ARG A 21 0.28 SIDE CHAIN
REMARK 500 4 ARG A 21 0.21 SIDE CHAIN
REMARK 500 5 ARG A 21 0.24 SIDE CHAIN
REMARK 500 6 ARG A 21 0.30 SIDE CHAIN
REMARK 500 7 ARG A 21 0.29 SIDE CHAIN
REMARK 500 8 ARG A 21 0.18 SIDE CHAIN
REMARK 500 9 ARG A 21 0.19 SIDE CHAIN
REMARK 500 10 ARG A 21 0.30 SIDE CHAIN
REMARK 500 11 ARG A 21 0.31 SIDE CHAIN
REMARK 500 12 ARG A 21 0.18 SIDE CHAIN
REMARK 500 13 ARG A 21 0.28 SIDE CHAIN
REMARK 500 14 ARG A 21 0.31 SIDE CHAIN
REMARK 500 15 ARG A 21 0.11 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1IY6 RELATED DB: PDB
REMARK 900 1IY6 CONTAINS OMSVP3 VARIANT, P14C/N39C
DBREF 1IY5 A 3 56 UNP P67954 IOVO_LOPNY 3 56
SEQRES 1 A 54 ALA VAL SER VAL ASP CYS SER GLU TYR PRO LYS PRO ALA
SEQRES 2 A 54 CYS THR MET GLU TYR ARG PRO LEU CYS GLY SER ASP ASN
SEQRES 3 A 54 LYS THR TYR GLY ASN LYS CYS ASN PHE CYS ASN ALA VAL
SEQRES 4 A 54 VAL GLU SER ASN GLY THR LEU THR LEU SER HIS PHE GLY
SEQRES 5 A 54 LYS CYS
HELIX 1 1 ASN A 33 ASN A 45 1 13
SHEET 1 A 3 LYS A 29 TYR A 31 0
SHEET 2 A 3 LEU A 23 GLY A 25 -1 N GLY A 25 O LYS A 29
SHEET 3 A 3 LEU A 50 HIS A 52 -1 O SER A 51 N CYS A 24
SSBOND 1 CYS A 8 CYS A 38 1555 1555 2.02
SSBOND 2 CYS A 16 CYS A 35 1555 1555 2.02
SSBOND 3 CYS A 24 CYS A 56 1555 1555 2.02
CISPEP 1 TYR A 11 PRO A 12 1 1.15
CISPEP 2 TYR A 11 PRO A 12 2 0.28
CISPEP 3 TYR A 11 PRO A 12 3 -0.06
CISPEP 4 TYR A 11 PRO A 12 4 0.55
CISPEP 5 TYR A 11 PRO A 12 5 0.50
CISPEP 6 TYR A 11 PRO A 12 6 0.71
CISPEP 7 TYR A 11 PRO A 12 7 0.37
CISPEP 8 TYR A 11 PRO A 12 8 0.05
CISPEP 9 TYR A 11 PRO A 12 9 0.73
CISPEP 10 TYR A 11 PRO A 12 10 0.35
CISPEP 11 TYR A 11 PRO A 12 11 0.19
CISPEP 12 TYR A 11 PRO A 12 12 0.01
CISPEP 13 TYR A 11 PRO A 12 13 -0.01
CISPEP 14 TYR A 11 PRO A 12 14 1.51
CISPEP 15 TYR A 11 PRO A 12 15 0.82
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