Header list of 1fyb.pdb file
Complete list - b 23 2 Bytes
HEADER HYDROLASE INHIBITOR 28-SEP-00 1FYB
TITLE SOLUTION STRUCTURE OF C1-T1, A TWO-DOMAIN PROTEINASE INHIBITOR DERIVED
TITLE 2 FROM THE CIRCULAR PRECURSOR PROTEIN NA-PROPI FROM NICOTIANA ALATA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEINASE INHIBITOR;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: DOMAINS 1 AND 2 (C1 AND T1) FROM THE SIX-DOMAIN PRECURSOR
COMPND 5 PROTEIN NA-PROPI;
COMPND 6 SYNONYM: NA-PROPI;
COMPND 7 ENGINEERED: YES
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;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PET11A
KEYWDS TWO-DOMAIN PROTEIN, HYDROLASE INHIBITOR
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR D.J.CRAIK,H.J.SCHIRRA,M.J.SCANLON,M.A.ANDERSON
REVDAT 4 23-FEB-22 1FYB 1 REMARK
REVDAT 3 24-FEB-09 1FYB 1 VERSN
REVDAT 2 01-APR-03 1FYB 1 JRNL
REVDAT 1 21-FEB-01 1FYB 0
JRNL AUTH H.J.SCHIRRA,M.J.SCANLON,M.C.LEE,M.A.ANDERSON,D.J.CRAIK
JRNL TITL THE SOLUTION STRUCTURE OF C1-T1, A TWO-DOMAIN PROTEINASE
JRNL TITL 2 INHIBITOR DERIVED FROM A CIRCULAR PRECURSOR PROTEIN FROM
JRNL TITL 3 NICOTIANA ALATA.
JRNL REF J.MOL.BIOL. V. 306 69 2001
JRNL REFN ISSN 0022-2836
JRNL PMID 11178894
JRNL DOI 10.1006/JMBI.2000.4318
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, X-PLOR 3.851
REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 1193 CONSTRAINTS, 1039 ARE NOE-DERIVED DISTANCE CONSTRAINTS, 82
REMARK 3 DIHEDRAL ANGLE RESTRAINTS, AND 72 HYDROGEN BOND DISTANCE
REMARK 3 CONSTRAINTS
REMARK 4
REMARK 4 1FYB COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-OCT-00.
REMARK 100 THE DEPOSITION ID IS D_1000012010.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 313; 313; 313
REMARK 210 PH : 5.8; 5.8; 5.8
REMARK 210 IONIC STRENGTH : 0; 0; 0
REMARK 210 PRESSURE : 1 ATM; 1 ATM; 1 ATM
REMARK 210 SAMPLE CONTENTS : 1MM C1-T1, UNLABELED; 1MM C1-T1,
REMARK 210 UNLABELED; 1MM C1-T1, U-15N,13C
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; DQF-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : DMX; ARX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 2.6, XEASY 1.3.7, DYANA
REMARK 210 1.5, X-PLOR 3.851
REMARK 210 METHOD USED : SIMULATED ANNEALING WITH TORSION
REMARK 210 ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 4
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D
REMARK 210 HOMONUCLEAR TECHNIQUES AND 3D HETERONUCLEAR 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: 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. = 8.1 DEGREES
REMARK 500 1 CYS A 108 CA - CB - SG ANGL. DEV. = 8.2 DEGREES
REMARK 500 2 CYS A 99 CA - CB - SG ANGL. DEV. = 10.6 DEGREES
REMARK 500 5 CYS A 50 CA - CB - SG ANGL. DEV. = 9.1 DEGREES
REMARK 500 6 CYS A 50 CA - CB - SG ANGL. DEV. = 7.1 DEGREES
REMARK 500 7 CYS A 108 CA - CB - SG ANGL. DEV. = 8.3 DEGREES
REMARK 500 8 CYS A 108 CA - CB - SG ANGL. DEV. = 7.6 DEGREES
REMARK 500 9 CYS A 50 CA - CB - SG ANGL. DEV. = 8.2 DEGREES
REMARK 500 11 CYS A 50 CA - CB - SG ANGL. DEV. = 8.4 DEGREES
REMARK 500 11 CYS A 66 CA - CB - SG ANGL. DEV. = 7.0 DEGREES
REMARK 500 12 CYS A 50 CA - CB - SG ANGL. DEV. = 7.5 DEGREES
REMARK 500 13 CYS A 50 CA - CB - SG ANGL. DEV. = 7.1 DEGREES
REMARK 500 14 CYS A 108 CA - CB - SG ANGL. DEV. = 7.8 DEGREES
REMARK 500 15 CYS A 37 CA - CB - SG ANGL. DEV. = 6.8 DEGREES
REMARK 500 16 CYS A 62 CA - CB - SG ANGL. DEV. = 7.2 DEGREES
REMARK 500 16 CYS A 83 CA - CB - SG ANGL. DEV. = 8.2 DEGREES
REMARK 500 16 CYS A 99 CA - CB - SG ANGL. DEV. = 7.3 DEGREES
REMARK 500 19 CYS A 41 CA - CB - SG ANGL. DEV. = 10.0 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 9 45.12 -89.22
REMARK 500 1 VAL A 24 -79.44 -127.56
REMARK 500 1 PRO A 31 75.22 -65.48
REMARK 500 1 ARG A 32 -53.43 -173.00
REMARK 500 1 THR A 38 -9.12 64.31
REMARK 500 1 ASN A 40 -177.77 47.42
REMARK 500 1 CYS A 41 119.36 48.63
REMARK 500 1 TYR A 47 -163.42 -166.23
REMARK 500 1 ARG A 52 -66.83 -152.92
REMARK 500 1 GLU A 54 8.09 -168.39
REMARK 500 1 LYS A 57 78.20 51.79
REMARK 500 1 ASN A 58 -39.82 -161.60
REMARK 500 1 ARG A 60 -73.59 7.29
REMARK 500 1 CYS A 66 -74.78 -90.65
REMARK 500 1 ALA A 67 35.57 -89.50
REMARK 500 1 VAL A 82 -77.91 -104.58
REMARK 500 1 PRO A 89 108.21 -38.58
REMARK 500 1 ALA A 94 103.29 -160.12
REMARK 500 1 PRO A 96 -5.70 -57.91
REMARK 500 1 ALA A 104 -61.32 -130.37
REMARK 500 2 LYS A 12 104.97 -48.16
REMARK 500 2 ASP A 20 -7.49 -59.69
REMARK 500 2 VAL A 24 -72.31 -128.89
REMARK 500 2 CYS A 37 -168.73 -79.96
REMARK 500 2 LEU A 39 64.66 -160.38
REMARK 500 2 ASN A 40 46.15 -88.65
REMARK 500 2 ASP A 42 88.35 -166.20
REMARK 500 2 TYR A 47 -163.07 -163.52
REMARK 500 2 LYS A 57 147.57 65.62
REMARK 500 2 ASN A 58 -78.76 64.48
REMARK 500 2 ASP A 59 166.67 61.98
REMARK 500 2 ILE A 61 85.39 -57.69
REMARK 500 2 CYS A 62 33.92 -93.26
REMARK 500 2 CYS A 66 -70.46 -89.38
REMARK 500 2 LYS A 70 86.91 -69.65
REMARK 500 2 VAL A 82 -78.38 -97.29
REMARK 500 2 PRO A 89 70.93 -67.95
REMARK 500 2 ARG A 90 -51.70 -162.88
REMARK 500 2 ASN A 98 -161.14 52.24
REMARK 500 2 CYS A 99 110.06 -36.67
REMARK 500 2 ALA A 104 -43.77 -131.78
REMARK 500 3 ARG A 2 -65.80 76.92
REMARK 500 3 CYS A 4 57.88 -140.61
REMARK 500 3 THR A 11 53.87 -153.11
REMARK 500 3 LYS A 12 -146.11 41.67
REMARK 500 3 ASP A 20 -8.01 -59.81
REMARK 500 3 VAL A 24 -71.29 -126.71
REMARK 500 3 CYS A 41 124.40 59.68
REMARK 500 3 ASP A 42 84.04 -152.33
REMARK 500 3 ALA A 46 -51.14 -125.37
REMARK 500
REMARK 500 THIS ENTRY HAS 432 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ASP A 88 PRO A 89 9 -145.12
REMARK 500 CYS A 108 PRO A 109 9 146.68
REMARK 500 CYS A 95 PRO A 96 12 148.48
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1FYB A 1 111 UNP Q40378 Q40378_NICAL 54 164
SEQRES 1 A 111 ASP ARG ILE CYS THR ASN CYS CYS ALA GLY THR LYS GLY
SEQRES 2 A 111 CYS LYS TYR PHE SER ASP ASP GLY THR PHE VAL CYS GLU
SEQRES 3 A 111 GLY GLU SER ASP PRO ARG ASN PRO LYS ALA CYS THR LEU
SEQRES 4 A 111 ASN CYS ASP PRO ARG ILE ALA TYR GLY VAL CYS PRO ARG
SEQRES 5 A 111 SER GLU GLU LYS LYS ASN ASP ARG ILE CYS THR ASN CYS
SEQRES 6 A 111 CYS ALA GLY THR LYS GLY CYS LYS TYR PHE SER ASP ASP
SEQRES 7 A 111 GLY THR PHE VAL CYS GLU GLY GLU SER ASP PRO ARG ASN
SEQRES 8 A 111 PRO LYS ALA CYS PRO ARG ASN CYS ASP PRO ARG ILE ALA
SEQRES 9 A 111 TYR GLY ILE CYS PRO LEU ALA
SHEET 1 A 3 THR A 22 PHE A 23 0
SHEET 2 A 3 LYS A 15 SER A 18 -1 N SER A 18 O THR A 22
SHEET 3 A 3 ILE A 45 VAL A 49 -1 N ALA A 46 O PHE A 17
SHEET 1 B 3 THR A 80 GLU A 84 0
SHEET 2 B 3 LYS A 73 SER A 76 -1 O TYR A 74 N CYS A 83
SHEET 3 B 3 ILE A 103 ILE A 107 -1 N ALA A 104 O PHE A 75
SSBOND 1 CYS A 4 CYS A 41 1555 1555 2.02
SSBOND 2 CYS A 7 CYS A 25 1555 1555 2.02
SSBOND 3 CYS A 8 CYS A 37 1555 1555 2.02
SSBOND 4 CYS A 14 CYS A 50 1555 1555 2.02
SSBOND 5 CYS A 62 CYS A 99 1555 1555 2.02
SSBOND 6 CYS A 65 CYS A 83 1555 1555 2.02
SSBOND 7 CYS A 66 CYS A 95 1555 1555 2.02
SSBOND 8 CYS A 72 CYS A 108 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 23 2 Bytes