Header list of 1a67.pdb file
Complete list - b 16 2 Bytes
HEADER PROTEINASE INHIBITOR 06-MAR-98 1A67
TITLE CHICKEN EGG WHITE CYSTATIN WILDTYPE, NMR, 16 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYSTATIN;
COMPND 3 CHAIN: A;
COMPND 4 OTHER_DETAILS: PHOSPHORYLATED
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 3 ORGANISM_COMMON: CHICKEN;
SOURCE 4 ORGANISM_TAXID: 9031;
SOURCE 5 ORGAN: EGG;
SOURCE 6 CELL: EGG;
SOURCE 7 CELLULAR_LOCATION: CYTOPLASM (WHITE)
KEYWDS PROTEINASE INHIBITOR, THIOL PROTEINASE, STEFFINS, KININOGENS
EXPDTA SOLUTION NMR
NUMMDL 16
AUTHOR T.DIECKMANN,L.MITSCHANG,M.HOFMANN,J.KOS,V.TURK,E.A.AUERSWALD,
AUTHOR 2 R.JAENICKE,H.OSCHKINAT
REVDAT 3 16-FEB-22 1A67 1 REMARK
REVDAT 2 24-FEB-09 1A67 1 VERSN
REVDAT 1 27-MAY-98 1A67 0
JRNL AUTH T.DIECKMANN,L.MITSCHANG,M.HOFMANN,J.KOS,V.TURK,
JRNL AUTH 2 E.A.AUERSWALD,R.JAENICKE,H.OSCHKINAT
JRNL TITL THE STRUCTURES OF NATIVE PHOSPHORYLATED CHICKEN CYSTATIN AND
JRNL TITL 2 OF A RECOMBINANT UNPHOSPHORYLATED VARIANT IN SOLUTION.
JRNL REF J.MOL.BIOL. V. 234 1048 1993
JRNL REFN ISSN 0022-2836
JRNL PMID 8263912
JRNL DOI 10.1006/JMBI.1993.1658
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH R.A.ENGH,T.DIECKMANN,W.BODE,E.A.AUERSWALD,V.TURK,R.HUBER,
REMARK 1 AUTH 2 H.OSCHKINAT
REMARK 1 TITL CONFORMATIONAL VARIABILITY OF CHICKEN CYSTATIN. COMPARISON
REMARK 1 TITL 2 OF STRUCTURES DETERMINED BY X-RAY DIFFRACTION AND NMR
REMARK 1 TITL 3 SPECTROSCOPY
REMARK 1 REF J.MOL.BIOL. V. 234 1060 1993
REMARK 1 REFN ISSN 0022-2836
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.0
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN THE
REMARK 3 JRNL CITATION ABOVE
REMARK 4
REMARK 4 1A67 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_1000170442.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 5.5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; COSY; TOCSY; 3D TOCSY
REMARK 210 -NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : AMX 500; AMX 600
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR 3.0
REMARK 210 METHOD USED : DISTANCE GEOMETRY AND SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 16
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST OVERALL ENERGY AND
REMARK 210 RESTRAINT VIOLATIONS
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 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (RES=RESIDUE NAME;
REMARK 470 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 470 MODELS 1-16
REMARK 470 RES CSSEQI ATOMS
REMARK 470 GLN A 116 O
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 ASN A 37 -90.65 38.26
REMARK 500 1 ASP A 38 -160.97 -53.35
REMARK 500 1 SER A 41 -27.94 97.54
REMARK 500 1 ARG A 43 139.15 -171.55
REMARK 500 1 VAL A 45 -75.56 -120.26
REMARK 500 1 SER A 49 177.39 173.68
REMARK 500 1 VAL A 55 66.26 -157.01
REMARK 500 1 SER A 56 -54.72 94.72
REMARK 500 1 THR A 69 177.73 179.39
REMARK 500 1 LYS A 73 -138.50 62.50
REMARK 500 1 SER A 74 -83.04 -69.02
REMARK 500 1 ASP A 77 -165.56 -110.44
REMARK 500 1 LEU A 78 -175.64 48.05
REMARK 500 1 GLN A 79 -108.09 -126.32
REMARK 500 1 SER A 80 -91.78 30.79
REMARK 500 1 CYS A 81 150.13 68.37
REMARK 500 1 GLU A 82 159.76 158.43
REMARK 500 1 PHE A 83 46.58 -82.98
REMARK 500 1 HIS A 84 85.40 69.32
REMARK 500 1 ASP A 85 -138.11 86.56
REMARK 500 1 LYS A 91 78.79 53.21
REMARK 500 1 ILE A 102 106.22 -162.39
REMARK 500 1 LEU A 105 17.72 -149.51
REMARK 500 1 ASN A 106 74.23 80.73
REMARK 500 1 ILE A 108 123.02 166.11
REMARK 500 1 GLU A 112 -174.72 174.43
REMARK 500 1 LYS A 114 87.03 -60.91
REMARK 500 2 ASN A 37 -91.97 26.42
REMARK 500 2 ASP A 38 -164.43 -53.50
REMARK 500 2 SER A 49 175.05 176.29
REMARK 500 2 VAL A 55 68.28 -161.52
REMARK 500 2 SER A 56 -51.29 89.21
REMARK 500 2 LYS A 73 -164.82 77.04
REMARK 500 2 SER A 74 -91.73 -75.52
REMARK 500 2 SER A 75 32.17 -159.04
REMARK 500 2 ASP A 77 173.98 83.95
REMARK 500 2 LEU A 78 173.46 54.46
REMARK 500 2 GLN A 79 -76.36 -118.53
REMARK 500 2 SER A 80 -147.48 60.96
REMARK 500 2 CYS A 81 -177.56 66.42
REMARK 500 2 PHE A 83 42.37 -82.41
REMARK 500 2 HIS A 84 88.46 81.35
REMARK 500 2 ASP A 85 -102.56 76.84
REMARK 500 2 GLU A 86 63.85 -165.90
REMARK 500 2 LYS A 91 87.31 52.21
REMARK 500 2 LEU A 105 22.98 -158.93
REMARK 500 2 ASN A 106 -82.39 177.34
REMARK 500 2 GLN A 107 -169.57 164.03
REMARK 500 2 GLU A 112 -170.90 168.82
REMARK 500 3 VAL A 14 132.71 -35.06
REMARK 500
REMARK 500 THIS ENTRY HAS 388 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 23 0.32 SIDE CHAIN
REMARK 500 1 ARG A 34 0.29 SIDE CHAIN
REMARK 500 1 ARG A 43 0.20 SIDE CHAIN
REMARK 500 1 ARG A 46 0.31 SIDE CHAIN
REMARK 500 1 ARG A 68 0.31 SIDE CHAIN
REMARK 500 2 ARG A 23 0.28 SIDE CHAIN
REMARK 500 2 ARG A 34 0.16 SIDE CHAIN
REMARK 500 2 ARG A 43 0.15 SIDE CHAIN
REMARK 500 2 ARG A 46 0.29 SIDE CHAIN
REMARK 500 2 ARG A 52 0.26 SIDE CHAIN
REMARK 500 2 ARG A 68 0.23 SIDE CHAIN
REMARK 500 3 ARG A 23 0.17 SIDE CHAIN
REMARK 500 3 ARG A 34 0.25 SIDE CHAIN
REMARK 500 3 ARG A 43 0.18 SIDE CHAIN
REMARK 500 3 ARG A 46 0.11 SIDE CHAIN
REMARK 500 3 ARG A 52 0.20 SIDE CHAIN
REMARK 500 3 ARG A 68 0.30 SIDE CHAIN
REMARK 500 4 ARG A 23 0.28 SIDE CHAIN
REMARK 500 4 ARG A 34 0.20 SIDE CHAIN
REMARK 500 4 ARG A 43 0.19 SIDE CHAIN
REMARK 500 4 ARG A 46 0.13 SIDE CHAIN
REMARK 500 4 ARG A 68 0.31 SIDE CHAIN
REMARK 500 5 ARG A 23 0.19 SIDE CHAIN
REMARK 500 5 ARG A 34 0.09 SIDE CHAIN
REMARK 500 5 ARG A 46 0.30 SIDE CHAIN
REMARK 500 5 ARG A 52 0.21 SIDE CHAIN
REMARK 500 5 ARG A 68 0.18 SIDE CHAIN
REMARK 500 6 ARG A 23 0.14 SIDE CHAIN
REMARK 500 6 ARG A 34 0.30 SIDE CHAIN
REMARK 500 6 ARG A 46 0.29 SIDE CHAIN
REMARK 500 6 ARG A 52 0.26 SIDE CHAIN
REMARK 500 6 ARG A 68 0.28 SIDE CHAIN
REMARK 500 7 ARG A 23 0.31 SIDE CHAIN
REMARK 500 7 ARG A 34 0.32 SIDE CHAIN
REMARK 500 7 ARG A 43 0.20 SIDE CHAIN
REMARK 500 7 ARG A 46 0.25 SIDE CHAIN
REMARK 500 7 ARG A 52 0.21 SIDE CHAIN
REMARK 500 7 ARG A 68 0.28 SIDE CHAIN
REMARK 500 8 ARG A 23 0.32 SIDE CHAIN
REMARK 500 8 ARG A 34 0.23 SIDE CHAIN
REMARK 500 8 ARG A 43 0.32 SIDE CHAIN
REMARK 500 8 ARG A 46 0.10 SIDE CHAIN
REMARK 500 8 ARG A 52 0.31 SIDE CHAIN
REMARK 500 8 ARG A 68 0.24 SIDE CHAIN
REMARK 500 9 ARG A 23 0.18 SIDE CHAIN
REMARK 500 9 ARG A 34 0.14 SIDE CHAIN
REMARK 500 9 ARG A 43 0.29 SIDE CHAIN
REMARK 500 9 ARG A 46 0.12 SIDE CHAIN
REMARK 500 9 ARG A 52 0.31 SIDE CHAIN
REMARK 500 9 ARG A 68 0.31 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 89 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1A67 A 9 116 UNP P01038 CYT_CHICK 32 139
SEQRES 1 A 108 GLY ALA PRO VAL PRO VAL ASP GLU ASN ASP GLU GLY LEU
SEQRES 2 A 108 GLN ARG ALA LEU GLN PHE ALA MET ALA GLU TYR ASN ARG
SEQRES 3 A 108 ALA SER ASN ASP LYS TYR SER SER ARG VAL VAL ARG VAL
SEQRES 4 A 108 ILE SER ALA LYS ARG GLN LEU VAL SER GLY ILE LYS TYR
SEQRES 5 A 108 ILE LEU GLN VAL GLU ILE GLY ARG THR THR CYS PRO LYS
SEQRES 6 A 108 SER SER GLY ASP LEU GLN SER CYS GLU PHE HIS ASP GLU
SEQRES 7 A 108 PRO GLU MET ALA LYS TYR THR THR CYS THR PHE VAL VAL
SEQRES 8 A 108 TYR SER ILE PRO TRP LEU ASN GLN ILE LYS LEU LEU GLU
SEQRES 9 A 108 SER LYS CYS GLN
HELIX 1 1 GLU A 19 ALA A 35 5 17
SHEET 1 A 4 ALA A 50 VAL A 55 0
SHEET 2 A 4 GLY A 57 ILE A 66 -1 N ILE A 61 O LYS A 51
SHEET 3 A 4 THR A 93 ILE A 102 -1 N SER A 101 O ILE A 58
SHEET 4 A 4 GLN A 107 LEU A 110 -1 N LYS A 109 O TYR A 100
SHEET 1 B 2 ARG A 43 VAL A 47 0
SHEET 2 B 2 VAL A 64 GLY A 67 -1 N GLY A 67 O ARG A 43
SSBOND 1 CYS A 71 CYS A 81 1555 1555 2.02
SSBOND 2 CYS A 95 CYS A 115 1555 1555 2.02
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