Header list of 1omt.pdb file
Complete list - b 23 2 Bytes
HEADER SERINE PROTEINASE INHIBITOR 11-OCT-95 1OMT
TITLE SOLUTION STRUCTURE OF OVOMUCOID (THIRD DOMAIN) FROM DOMESTIC TURKEY
TITLE 2 (298K, PH 4.1) (NMR, 50 STRUCTURES) (STANDARD NOESY ANALYSIS)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: OVOMUCOID (THIRD DOMAIN);
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: OMTKY3
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MELEAGRIS GALLOPAVO;
SOURCE 3 ORGANISM_COMMON: TURKEY;
SOURCE 4 ORGANISM_TAXID: 9103;
SOURCE 5 CELLULAR_LOCATION: EGG WHITE
KEYWDS SPIN DIFFUSION, NETWORK EDITING, BD-NOESY, CBD-NOESY, SERINE
KEYWDS 2 PROTEINASE INHIBITOR
EXPDTA SOLUTION NMR
NUMMDL 50
AUTHOR C.G.HOOGSTRATEN,S.CHOE,W.M.WESTLER,J.L.MARKLEY
REVDAT 3 23-FEB-22 1OMT 1 REMARK
REVDAT 2 24-FEB-09 1OMT 1 VERSN
REVDAT 1 08-MAR-96 1OMT 0
JRNL AUTH C.G.HOOGSTRATEN,S.CHOE,W.M.WESTLER,J.L.MARKLEY
JRNL TITL COMPARISON OF THE ACCURACY OF PROTEIN SOLUTION STRUCTURES
JRNL TITL 2 DERIVED FROM CONVENTIONAL AND NETWORK-EDITED NOESY DATA.
JRNL REF PROTEIN SCI. V. 4 2289 1995
JRNL REFN ISSN 0961-8368
JRNL PMID 8563625
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH A.M.KREZEL,P.DARBA,A.D.ROBERTSON,J.FEJZO,S.MACURA,
REMARK 1 AUTH 2 J.L.MARKLEY
REMARK 1 TITL SOLUTION STRUCTURE OF TURKEY OVOMUCOID THIRD DOMAIN AS
REMARK 1 TITL 2 DETERMINED FROM NUCLEAR MAGNETIC RESONANCE DATA
REMARK 1 REF J.MOL.BIOL. V. 242 203 1994
REMARK 1 REFN ISSN 0022-2836
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1OMT 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_1000175477.
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 : 50
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: 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: 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 17 TYR A 31 CB - CG - CD2 ANGL. DEV. = -3.7 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 ALA A 2 60.86 -101.56
REMARK 500 1 ALA A 3 -166.79 -117.34
REMARK 500 1 GLU A 10 42.02 -106.06
REMARK 500 1 THR A 17 -169.29 -63.79
REMARK 500 1 ARG A 21 82.26 -162.57
REMARK 500 1 ASN A 28 37.91 79.89
REMARK 500 1 ASN A 33 -166.64 -163.83
REMARK 500 1 LEU A 48 -71.45 -83.00
REMARK 500 1 THR A 49 138.35 60.78
REMARK 500 2 ALA A 2 -170.21 48.36
REMARK 500 2 ALA A 3 84.89 49.15
REMARK 500 2 SER A 5 130.33 -177.48
REMARK 500 2 CYS A 8 50.45 -97.91
REMARK 500 2 GLU A 10 43.18 -101.94
REMARK 500 2 ALA A 15 151.12 179.57
REMARK 500 2 THR A 17 -144.88 -64.62
REMARK 500 2 ASN A 28 16.50 84.83
REMARK 500 2 ASN A 33 -162.87 -162.41
REMARK 500 2 LEU A 48 -78.37 -82.41
REMARK 500 2 THR A 49 172.85 77.69
REMARK 500 3 ALA A 2 63.71 61.76
REMARK 500 3 SER A 5 124.20 -174.53
REMARK 500 3 CYS A 8 39.70 -156.20
REMARK 500 3 THR A 17 -176.17 -52.51
REMARK 500 3 ARG A 21 71.24 -160.54
REMARK 500 3 ASN A 28 10.15 88.97
REMARK 500 3 ASN A 33 -149.73 -172.47
REMARK 500 3 THR A 49 125.21 52.28
REMARK 500 3 HIS A 52 162.04 173.68
REMARK 500 4 ALA A 2 -44.93 -151.07
REMARK 500 4 ALA A 3 178.02 -59.01
REMARK 500 4 GLU A 10 30.16 -94.69
REMARK 500 4 ALA A 15 126.18 -174.93
REMARK 500 4 THR A 17 -150.26 -64.70
REMARK 500 4 ARG A 21 74.54 -151.41
REMARK 500 4 ASN A 28 30.40 85.29
REMARK 500 4 ASN A 33 -166.08 -162.50
REMARK 500 4 LEU A 48 -79.77 -79.74
REMARK 500 4 THR A 49 136.52 95.57
REMARK 500 5 ALA A 2 -174.62 -59.91
REMARK 500 5 SER A 5 149.59 175.01
REMARK 500 5 CYS A 8 42.06 -144.70
REMARK 500 5 ALA A 15 128.37 -170.83
REMARK 500 5 THR A 17 -177.62 -61.71
REMARK 500 5 ASN A 28 19.60 83.15
REMARK 500 5 THR A 49 126.34 57.66
REMARK 500 5 HIS A 52 163.47 154.46
REMARK 500 6 THR A 17 -164.74 -59.78
REMARK 500 6 ASN A 28 30.32 77.27
REMARK 500 6 ASN A 33 -157.06 -162.58
REMARK 500
REMARK 500 THIS ENTRY HAS 430 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 0.15 SIDE CHAIN
REMARK 500 2 ARG A 21 0.15 SIDE CHAIN
REMARK 500 3 ARG A 21 0.20 SIDE CHAIN
REMARK 500 4 ARG A 21 0.30 SIDE CHAIN
REMARK 500 5 ARG A 21 0.15 SIDE CHAIN
REMARK 500 6 ARG A 21 0.21 SIDE CHAIN
REMARK 500 7 ARG A 21 0.31 SIDE CHAIN
REMARK 500 9 ARG A 21 0.32 SIDE CHAIN
REMARK 500 10 ARG A 21 0.32 SIDE CHAIN
REMARK 500 11 ARG A 21 0.32 SIDE CHAIN
REMARK 500 12 ARG A 21 0.17 SIDE CHAIN
REMARK 500 13 ARG A 21 0.32 SIDE CHAIN
REMARK 500 14 ARG A 21 0.32 SIDE CHAIN
REMARK 500 15 ARG A 21 0.27 SIDE CHAIN
REMARK 500 16 ARG A 21 0.23 SIDE CHAIN
REMARK 500 17 ARG A 21 0.09 SIDE CHAIN
REMARK 500 18 ARG A 21 0.16 SIDE CHAIN
REMARK 500 19 ARG A 21 0.32 SIDE CHAIN
REMARK 500 20 ARG A 21 0.23 SIDE CHAIN
REMARK 500 21 ARG A 21 0.31 SIDE CHAIN
REMARK 500 22 ARG A 21 0.31 SIDE CHAIN
REMARK 500 23 ARG A 21 0.14 SIDE CHAIN
REMARK 500 25 ARG A 21 0.31 SIDE CHAIN
REMARK 500 26 ARG A 21 0.29 SIDE CHAIN
REMARK 500 27 ARG A 21 0.11 SIDE CHAIN
REMARK 500 28 ARG A 21 0.24 SIDE CHAIN
REMARK 500 29 ARG A 21 0.24 SIDE CHAIN
REMARK 500 30 ARG A 21 0.27 SIDE CHAIN
REMARK 500 31 ARG A 21 0.32 SIDE CHAIN
REMARK 500 32 ARG A 21 0.20 SIDE CHAIN
REMARK 500 33 ARG A 21 0.29 SIDE CHAIN
REMARK 500 34 ARG A 21 0.20 SIDE CHAIN
REMARK 500 35 ARG A 21 0.22 SIDE CHAIN
REMARK 500 36 ARG A 21 0.31 SIDE CHAIN
REMARK 500 37 ARG A 21 0.29 SIDE CHAIN
REMARK 500 38 ARG A 21 0.29 SIDE CHAIN
REMARK 500 39 ARG A 21 0.24 SIDE CHAIN
REMARK 500 40 ARG A 21 0.09 SIDE CHAIN
REMARK 500 41 ARG A 21 0.29 SIDE CHAIN
REMARK 500 42 ARG A 21 0.31 SIDE CHAIN
REMARK 500 43 ARG A 21 0.20 SIDE CHAIN
REMARK 500 44 ARG A 21 0.31 SIDE CHAIN
REMARK 500 45 ARG A 21 0.12 SIDE CHAIN
REMARK 500 46 ARG A 21 0.24 SIDE CHAIN
REMARK 500 47 ARG A 21 0.29 SIDE CHAIN
REMARK 500 48 ARG A 21 0.10 SIDE CHAIN
REMARK 500 49 ARG A 21 0.11 SIDE CHAIN
REMARK 500 50 ARG A 21 0.23 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: REA
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
DBREF 1OMT A 1 56 UNP P68390 IOVO_MELGA 130 185
SEQRES 1 A 56 LEU ALA ALA VAL SER VAL ASP CYS SER GLU TYR PRO LYS
SEQRES 2 A 56 PRO ALA CYS THR LEU GLU TYR ARG PRO LEU CYS GLY SER
SEQRES 3 A 56 ASP ASN LYS THR TYR GLY ASN LYS CYS ASN PHE CYS ASN
SEQRES 4 A 56 ALA VAL VAL GLU SER ASN GLY THR LEU THR LEU SER HIS
SEQRES 5 A 56 PHE GLY LYS CYS
HELIX 1 1 CYS A 8 GLU A 10 5 3
HELIX 2 2 LYS A 34 SER A 44 1 11
SHEET 1 A 2 LEU A 23 GLY A 25 0
SHEET 2 A 2 LEU A 50 PHE A 53 -1 N HIS A 52 O 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 1.12
CISPEP 2 TYR A 11 PRO A 12 2 -0.23
CISPEP 3 TYR A 11 PRO A 12 3 1.24
CISPEP 4 TYR A 11 PRO A 12 4 0.15
CISPEP 5 TYR A 11 PRO A 12 5 1.90
CISPEP 6 TYR A 11 PRO A 12 6 0.91
CISPEP 7 TYR A 11 PRO A 12 7 1.97
CISPEP 8 TYR A 11 PRO A 12 8 2.23
CISPEP 9 TYR A 11 PRO A 12 9 3.12
CISPEP 10 TYR A 11 PRO A 12 10 2.14
CISPEP 11 TYR A 11 PRO A 12 11 2.19
CISPEP 12 TYR A 11 PRO A 12 12 2.21
CISPEP 13 TYR A 11 PRO A 12 13 2.96
CISPEP 14 TYR A 11 PRO A 12 14 2.59
CISPEP 15 TYR A 11 PRO A 12 15 2.37
CISPEP 16 TYR A 11 PRO A 12 16 1.80
CISPEP 17 TYR A 11 PRO A 12 17 2.19
CISPEP 18 TYR A 11 PRO A 12 18 2.10
CISPEP 19 TYR A 11 PRO A 12 19 1.99
CISPEP 20 TYR A 11 PRO A 12 20 2.20
CISPEP 21 TYR A 11 PRO A 12 21 2.25
CISPEP 22 TYR A 11 PRO A 12 22 2.45
CISPEP 23 TYR A 11 PRO A 12 23 1.47
CISPEP 24 TYR A 11 PRO A 12 24 3.47
CISPEP 25 TYR A 11 PRO A 12 25 0.21
CISPEP 26 TYR A 11 PRO A 12 26 3.15
CISPEP 27 TYR A 11 PRO A 12 27 1.85
CISPEP 28 TYR A 11 PRO A 12 28 3.19
CISPEP 29 TYR A 11 PRO A 12 29 2.04
CISPEP 30 TYR A 11 PRO A 12 30 3.07
CISPEP 31 TYR A 11 PRO A 12 31 1.95
CISPEP 32 TYR A 11 PRO A 12 32 2.07
CISPEP 33 TYR A 11 PRO A 12 33 1.91
CISPEP 34 TYR A 11 PRO A 12 34 1.61
CISPEP 35 TYR A 11 PRO A 12 35 2.93
CISPEP 36 TYR A 11 PRO A 12 36 2.11
CISPEP 37 TYR A 11 PRO A 12 37 2.36
CISPEP 38 TYR A 11 PRO A 12 38 2.70
CISPEP 39 TYR A 11 PRO A 12 39 0.94
CISPEP 40 TYR A 11 PRO A 12 40 2.30
CISPEP 41 TYR A 11 PRO A 12 41 2.03
CISPEP 42 TYR A 11 PRO A 12 42 1.71
CISPEP 43 TYR A 11 PRO A 12 43 1.80
CISPEP 44 TYR A 11 PRO A 12 44 2.49
CISPEP 45 TYR A 11 PRO A 12 45 2.48
CISPEP 46 TYR A 11 PRO A 12 46 1.22
CISPEP 47 TYR A 11 PRO A 12 47 1.51
CISPEP 48 TYR A 11 PRO A 12 48 0.71
CISPEP 49 TYR A 11 PRO A 12 49 0.84
CISPEP 50 TYR A 11 PRO A 12 50 2.23
SITE 1 REA 2 LEU A 18 GLU A 19
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 23 2 Bytes