Header list of 1ce3.pdb file
Complete list - v 3 2 Bytes
HEADER PROTEASE INHIBITOR 14-MAR-99 1CE3
TITLE PUTATIVE ANCESTRAL PROTEIN ENCODED BY A SINGLE SEQUENCE REPEAT OF THE
TITLE 2 MULTIDOMAIN PROTEINASE INHIBITOR FROM NICOTIANA ALATA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: API;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: FIRST SEQUENCE REPEAT;
COMPND 5 ENGINEERED: YES;
COMPND 6 OTHER_DETAILS: SINGLE SEQUENCE REPEAT FROM A MULTIDOMAIN PROTEINASE
COMPND 7 INHIBITOR
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: NICOTIANA ALATA;
SOURCE 3 ORGANISM_COMMON: PERSIAN TOBACCO;
SOURCE 4 ORGANISM_TAXID: 4087;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PROTEASE INHIBITOR, CIRCULAR PERMUTATION, NICOTIANA ALATA
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR M.J.SCANLON,M.C.S.LEE,M.A.ANDERSON,D.J.CRAIK
REVDAT 5 03-NOV-21 1CE3 1 COMPND REMARK
REVDAT 4 24-FEB-09 1CE3 1 VERSN
REVDAT 3 01-APR-03 1CE3 1 JRNL
REVDAT 2 01-SEP-99 1CE3 1 JRNL
REVDAT 1 27-MAR-99 1CE3 0
JRNL AUTH M.J.SCANLON,M.C.LEE,M.A.ANDERSON,D.J.CRAIK
JRNL TITL STRUCTURE OF A PUTATIVE ANCESTRAL PROTEIN ENCODED BY A
JRNL TITL 2 SINGLE SEQUENCE REPEAT FROM A MULTIDOMAIN PROTEINASE
JRNL TITL 3 INHIBITOR GENE FROM NICOTIANA ALATA.
JRNL REF STRUCTURE FOLD.DES. V. 7 793 1999
JRNL REFN ISSN 0969-2126
JRNL PMID 10425681
JRNL DOI 10.1016/S0969-2126(99)80103-8
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.85
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN THE
REMARK 3 STRUCTURE CITATION ABOVE
REMARK 4
REMARK 4 1CE3 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-MAR-99.
REMARK 100 THE DEPOSITION ID IS D_1000000650.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 313
REMARK 210 PH : 5.8
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 1 MM PEPTIDE
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : DQFCOSY; ECOSY; TOCSY; NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : DRX; ARX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XEASY, DYANA, X-PLOR
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATIONS AND
REMARK 210 LOWEST ENERGY
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 1 CYS A 50 CA - CB - SG ANGL. DEV. = 12.6 DEGREES
REMARK 500 2 CYS A 50 CA - CB - SG ANGL. DEV. = 6.9 DEGREES
REMARK 500 3 CYS A 29 CA - CB - SG ANGL. DEV. = 9.0 DEGREES
REMARK 500 9 CYS A 8 CA - CB - SG ANGL. DEV. = 8.3 DEGREES
REMARK 500 9 CYS A 29 CA - CB - SG ANGL. DEV. = 7.5 DEGREES
REMARK 500 12 CYS A 33 CA - CB - SG ANGL. DEV. = 8.2 DEGREES
REMARK 500 15 CYS A 8 CA - CB - SG ANGL. DEV. = 7.5 DEGREES
REMARK 500 15 CYS A 50 CA - CB - SG ANGL. DEV. = 7.0 DEGREES
REMARK 500 17 CYS A 8 CA - CB - SG ANGL. DEV. = 7.6 DEGREES
REMARK 500 17 CYS A 29 CA - CB - SG ANGL. DEV. = 7.7 DEGREES
REMARK 500 20 CYS A 8 CA - CB - SG ANGL. DEV. = 10.6 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 LYS A 2 95.39 -66.93
REMARK 500 1 ASN A 7 170.10 -56.25
REMARK 500 1 ARG A 19 72.87 62.13
REMARK 500 1 GLU A 21 -123.28 -74.42
REMARK 500 1 GLU A 22 143.11 70.32
REMARK 500 1 LYS A 24 57.58 -95.39
REMARK 500 1 ASN A 25 81.52 -178.41
REMARK 500 1 ASP A 26 108.40 -163.06
REMARK 500 1 VAL A 49 -77.88 -103.45
REMARK 500 1 GLU A 53 28.95 -165.86
REMARK 500 2 ALA A 3 96.40 -59.02
REMARK 500 2 CYS A 4 -167.70 -64.04
REMARK 500 2 THR A 5 -21.86 -38.49
REMARK 500 2 LEU A 6 6.89 53.46
REMARK 500 2 SER A 20 65.22 -172.26
REMARK 500 2 GLU A 21 -88.31 -73.69
REMARK 500 2 GLU A 22 136.87 66.98
REMARK 500 2 LYS A 24 115.91 71.24
REMARK 500 2 ASN A 25 47.65 -147.26
REMARK 500 2 ASP A 26 130.93 -171.66
REMARK 500 2 ILE A 28 -177.50 -64.08
REMARK 500 2 GLU A 53 29.66 -171.28
REMARK 500 3 ALA A 3 119.28 53.84
REMARK 500 3 CYS A 4 -175.02 -59.80
REMARK 500 3 THR A 5 155.63 -45.51
REMARK 500 3 LEU A 6 2.20 -62.60
REMARK 500 3 ASN A 7 -176.25 -61.71
REMARK 500 3 ALA A 13 -63.74 -105.11
REMARK 500 3 GLU A 21 -108.15 35.25
REMARK 500 3 GLU A 22 115.69 53.94
REMARK 500 3 ASN A 25 16.85 -155.12
REMARK 500 3 GLU A 53 57.46 -166.59
REMARK 500 4 ALA A 3 143.91 173.03
REMARK 500 4 CYS A 4 -164.29 -68.43
REMARK 500 4 THR A 5 1.97 -60.82
REMARK 500 4 ALA A 13 -60.62 -109.60
REMARK 500 4 SER A 20 58.17 -155.39
REMARK 500 4 GLU A 21 -77.50 -74.48
REMARK 500 4 GLU A 22 162.30 60.27
REMARK 500 4 LYS A 23 92.62 -59.95
REMARK 500 4 ASN A 25 43.57 -147.62
REMARK 500 4 CYS A 29 76.56 -103.25
REMARK 500 4 VAL A 49 -61.57 -104.07
REMARK 500 4 GLU A 51 54.16 -94.67
REMARK 500 4 GLU A 53 61.36 169.67
REMARK 500 5 ALA A 3 130.59 65.22
REMARK 500 5 LEU A 6 17.05 52.24
REMARK 500 5 TYR A 14 -169.62 -165.46
REMARK 500 5 PRO A 18 164.65 -36.55
REMARK 500 5 SER A 20 113.94 178.34
REMARK 500
REMARK 500 THIS ENTRY HAS 220 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1CE3 A 1 54 UNP Q40378 Q40378_NICAL 29 82
SEQRES 1 A 54 MET LYS ALA CYS THR LEU ASN CYS ASP PRO ARG ILE ALA
SEQRES 2 A 54 TYR GLY VAL CYS PRO ARG SER GLU GLU LYS LYS ASN ASP
SEQRES 3 A 54 ARG ILE CYS THR ASN CYS CYS ALA GLY THR LYS GLY CYS
SEQRES 4 A 54 LYS TYR PHE SER ASP ASP GLY THR PHE VAL CYS GLU GLY
SEQRES 5 A 54 GLU SER
SHEET 1 A 2 TYR A 14 VAL A 16 0
SHEET 2 A 2 LYS A 40 PHE A 42 -1 N PHE A 42 O TYR A 14
SSBOND 1 CYS A 4 CYS A 33 1555 1555 2.02
SSBOND 2 CYS A 8 CYS A 29 1555 1555 2.02
SSBOND 3 CYS A 17 CYS A 39 1555 1555 2.02
SSBOND 4 CYS A 32 CYS A 50 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 - v 3 2 Bytes