Header list of 1m8b.pdb file
Complete list - t 27 2 Bytes
HEADER HYDROLASE INHIBITOR 24-JUL-02 1M8B
TITLE SOLUTION STRUCTURE OF THE C STATE OF TURKEY OVOMUCOID AT PH 2.5
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: OVOMUCOID;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 130-185; KAZAL-LIKE 3 (INHIBIT CHYMOTRYPIN,
COMPND 5 ELASTASE, ETC.);
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THE SEQUENCE FOR OVOMUCOID FRAGMENT WAS CHEMICALLY
SOURCE 4 SYNTHESIZED. IT OCCURS NATURALLY IN MELEAGRIS GALLOPAVO (COMMON
SOURCE 5 TURKEY).
KEYWDS OMTKY3 CONFORMATIONAL TRANSITION CIS-TRANS ISOMERIZATION, HYDROLASE
KEYWDS 2 INHIBITOR
EXPDTA SOLUTION NMR
NUMMDL 20
MDLTYP MINIMIZED AVERAGE
AUTHOR J.SONG,M.LASKOWSKI JR.,M.A.QASIM,J.L.MARKLEY
REVDAT 4 27-OCT-21 1M8B 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1M8B 1 VERSN
REVDAT 2 17-MAY-05 1M8B 3 ATOM JRNL
REVDAT 1 04-SEP-02 1M8B 0
JRNL AUTH J.SONG,M.LASKOWSKI JR,M.A.QASIM,J.L.MARKLEY
JRNL TITL TWO CONFORMATIONAL STATES OF TURKEY OVOMUCOID THIRD DOMAIN
JRNL TITL 2 AT LOW PH: THREE-DIMENSIONAL STRUCTURES, INTERNAL DYNAMICS,
JRNL TITL 3 AND INTERCONVERSION KINETICS AND THERMODYNAMICS.
JRNL REF BIOCHEMISTRY V. 42 6380 2003
JRNL REFN ISSN 0006-2960
JRNL PMID 12767219
JRNL DOI 10.1021/BI034053F
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : FELIX 95, DYANA 1.5
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1M8B COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-JUL-02.
REMARK 100 THE DEPOSITION ID IS D_1000016721.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 2.5
REMARK 210 IONIC STRENGTH : NO SALT ADDED
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1 MM; 1 MM
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ; 600 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : DMX; AMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : SPARKY 3.72, DYANA 1.5
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS,SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH FAVORABLE NON
REMARK 210 -BOND ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
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: 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 ALA A 2 73.03 45.63
REMARK 500 1 CYS A 8 25.69 -155.07
REMARK 500 1 GLU A 10 22.51 -153.67
REMARK 500 1 ASP A 14 54.88 -95.13
REMARK 500 1 SER A 44 35.26 -93.42
REMARK 500 1 ASN A 45 17.70 57.00
REMARK 500 2 ALA A 3 -161.09 41.68
REMARK 500 2 CYS A 8 26.50 -151.48
REMARK 500 2 SER A 9 42.40 -100.03
REMARK 500 2 GLU A 10 27.17 -161.03
REMARK 500 2 ASN A 28 39.99 71.03
REMARK 500 2 HIS A 52 -179.38 -171.09
REMARK 500 3 ALA A 2 -178.49 57.68
REMARK 500 3 VAL A 4 -180.00 50.90
REMARK 500 3 SER A 5 119.77 -179.98
REMARK 500 3 CYS A 8 25.94 -155.26
REMARK 500 3 GLU A 10 15.95 -143.86
REMARK 500 4 ALA A 2 171.11 62.62
REMARK 500 4 SER A 5 108.50 -178.79
REMARK 500 4 GLU A 10 28.55 -165.77
REMARK 500 4 ASP A 14 48.21 -88.29
REMARK 500 4 ALA A 15 174.04 175.77
REMARK 500 4 SER A 44 46.68 -85.67
REMARK 500 5 VAL A 4 178.19 50.32
REMARK 500 5 SER A 5 143.69 -178.26
REMARK 500 5 CYS A 8 35.32 -149.51
REMARK 500 5 SER A 9 46.18 -104.14
REMARK 500 5 GLU A 10 33.54 -173.40
REMARK 500 5 ALA A 15 160.41 179.66
REMARK 500 5 SER A 44 41.68 -88.86
REMARK 500 5 ASN A 45 24.18 48.71
REMARK 500 6 ALA A 2 114.24 -176.06
REMARK 500 6 ALA A 3 58.68 178.72
REMARK 500 6 VAL A 4 179.58 50.70
REMARK 500 6 SER A 5 151.67 179.27
REMARK 500 6 GLU A 10 -38.97 -172.66
REMARK 500 6 TYR A 11 155.62 -37.39
REMARK 500 6 ASP A 14 46.59 -96.22
REMARK 500 6 ALA A 15 165.16 174.95
REMARK 500 6 SER A 44 39.45 -90.03
REMARK 500 6 ASN A 45 15.76 59.71
REMARK 500 7 GLU A 10 -39.99 -164.88
REMARK 500 7 TYR A 11 159.59 -38.22
REMARK 500 7 LYS A 55 137.02 -39.94
REMARK 500 8 ALA A 2 178.05 65.01
REMARK 500 8 ALA A 3 141.72 66.80
REMARK 500 8 CYS A 8 35.34 -155.94
REMARK 500 8 SER A 9 41.19 -101.66
REMARK 500 8 GLU A 10 27.06 -161.00
REMARK 500 8 SER A 44 37.66 -89.96
REMARK 500
REMARK 500 THIS ENTRY HAS 139 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1M8C RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE T STATE OF TURKEY OVOMUCOID AT PH 2.5
DBREF 1M8B A 1 56 UNP P01004 IOVO_MELGA 130 185
SEQADV 1M8B ASP A 14 UNP P01004 PRO 143 ENGINEERED MUTATION
SEQRES 1 A 56 LEU ALA ALA VAL SER VAL ASP CYS SER GLU TYR PRO LYS
SEQRES 2 A 56 ASP 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 ASN A 33 SER A 44 1 12
SHEET 1 A 3 THR A 30 TYR A 31 0
SHEET 2 A 3 LEU A 23 GLY A 25 -1 N LEU A 23 O TYR A 31
SHEET 3 A 3 LEU A 50 PHE A 53 -1 O HIS A 52 N CYS A 24
SSBOND 1 CYS A 8 CYS A 38 1555 1555 2.09
SSBOND 2 CYS A 16 CYS A 35 1555 1555 2.00
SSBOND 3 CYS A 24 CYS A 56 1555 1555 2.09
CISPEP 1 TYR A 11 PRO A 12 1 0.04
CISPEP 2 TYR A 11 PRO A 12 2 0.02
CISPEP 3 TYR A 11 PRO A 12 3 0.02
CISPEP 4 TYR A 11 PRO A 12 4 -0.09
CISPEP 5 TYR A 11 PRO A 12 5 -0.04
CISPEP 6 TYR A 11 PRO A 12 6 -0.02
CISPEP 7 TYR A 11 PRO A 12 7 -0.04
CISPEP 8 TYR A 11 PRO A 12 8 0.04
CISPEP 9 TYR A 11 PRO A 12 9 -0.06
CISPEP 10 TYR A 11 PRO A 12 10 -0.04
CISPEP 11 TYR A 11 PRO A 12 11 -0.14
CISPEP 12 TYR A 11 PRO A 12 12 -0.04
CISPEP 13 TYR A 11 PRO A 12 13 0.11
CISPEP 14 TYR A 11 PRO A 12 14 0.04
CISPEP 15 TYR A 11 PRO A 12 15 0.00
CISPEP 16 TYR A 11 PRO A 12 16 -0.02
CISPEP 17 TYR A 11 PRO A 12 17 0.03
CISPEP 18 TYR A 11 PRO A 12 18 0.01
CISPEP 19 TYR A 11 PRO A 12 19 -0.02
CISPEP 20 TYR A 11 PRO A 12 20 -0.03
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 - t 27 2 Bytes