Header list of 1kma.pdb file
Complete list - b 23 2 Bytes
HEADER BLOOD CLOTTING 14-DEC-01 1KMA
TITLE NMR STRUCTURE OF THE DOMAIN-I OF THE KAZAL-TYPE THROMBIN INHIBITOR
TITLE 2 DIPETALIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIPETALIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: N-TERMINAL DOMAIN-I;
COMPND 5 SYNONYM: DIPETALOGASTIN;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DIPETALOGASTER MAXIMUS;
SOURCE 3 ORGANISM_TAXID: 72496;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: TG1;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PMEX6
KEYWDS DISULPHIDE-RICH SMALL ALPHA+BETA FOLD, KAZAL-TYPE, BLOOD CLOTTING
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR B.SCHLOTT,J.WOHNERT,C.ICKE,M.HARTMANN,R.RAMACHANDRAN,K.-H.GUHRS,
AUTHOR 2 E.GLUSA,J.FLEMMING,M.GORLACH,F.GROSSE,O.OHLENSCHLAGER
REVDAT 4 23-FEB-22 1KMA 1 REMARK
REVDAT 3 24-FEB-09 1KMA 1 VERSN
REVDAT 2 01-APR-03 1KMA 1 JRNL
REVDAT 1 15-MAY-02 1KMA 0
JRNL AUTH B.SCHLOTT,J.WOHNERT,C.ICKE,M.HARTMANN,R.RAMACHANDRAN,
JRNL AUTH 2 K.H.GUHRS,E.GLUSA,J.FLEMMING,M.GORLACH,F.GROSSE,
JRNL AUTH 3 O.OHLENSCHLAGER
JRNL TITL INTERACTION OF KAZAL-TYPE INHIBITOR DOMAINS WITH SERINE
JRNL TITL 2 PROTEINASES: BIOCHEMICAL AND STRUCTURAL STUDIES.
JRNL REF J.MOL.BIOL. V. 318 533 2002
JRNL REFN ISSN 0022-2836
JRNL PMID 12051857
JRNL DOI 10.1016/S0022-2836(02)00014-1
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA 1.5, OPAL 2.6
REMARK 3 AUTHORS : GUENTERT (DYANA), LUGINBUEHL (OPAL)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 1122 DISTANCE CONSTRAINTS AND 239 DIHEDRAL ANGLE RESTRAINTS.
REMARK 4
REMARK 4 1KMA COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-DEC-01.
REMARK 100 THE DEPOSITION ID IS D_1000015104.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 288
REMARK 210 PH : 6.68
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM DIPETALIN-I U-15N; 1.37MM
REMARK 210 DIPETALIN-I U-15N,13C
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; HNHA
REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : DISTANCE GEOMETRY/SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 16
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY.
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: 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 4 ARG A 14 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 5 CYS A 31 CA - CB - SG ANGL. DEV. = 7.8 DEGREES
REMARK 500 8 ARG A 14 NE - CZ - NH2 ANGL. DEV. = 3.7 DEGREES
REMARK 500 9 ARG A 14 NE - CZ - NH2 ANGL. DEV. = 3.2 DEGREES
REMARK 500 12 CYS A 31 CA - CB - SG ANGL. DEV. = 8.1 DEGREES
REMARK 500 16 ARG A 14 NE - CZ - NH2 ANGL. DEV. = 4.5 DEGREES
REMARK 500 18 ARG A 14 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 19 CYS A 31 CA - CB - SG ANGL. DEV. = 7.6 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 GLN A 2 133.75 -176.13
REMARK 500 1 GLU A 7 -24.33 -154.47
REMARK 500 1 CYS A 8 158.35 -49.61
REMARK 500 1 ARG A 10 43.65 -80.29
REMARK 500 1 LEU A 12 42.79 -76.96
REMARK 500 1 ASP A 19 0.00 -69.02
REMARK 500 1 HIS A 44 151.31 166.12
REMARK 500 1 GLU A 45 -173.26 -68.34
REMARK 500 1 HIS A 51 34.51 -167.45
REMARK 500 1 ASP A 52 -167.54 -173.28
REMARK 500 1 HIS A 53 45.98 -153.39
REMARK 500 2 GLN A 2 -89.88 -171.39
REMARK 500 2 ARG A 10 43.56 -84.81
REMARK 500 2 LEU A 12 43.77 -76.89
REMARK 500 2 HIS A 13 58.01 -92.36
REMARK 500 2 ASN A 21 96.99 -66.71
REMARK 500 2 CYS A 48 -77.47 -83.47
REMARK 500 2 GLU A 50 -72.32 162.78
REMARK 500 2 HIS A 53 53.41 -161.71
REMARK 500 3 GLN A 2 -86.56 -176.70
REMARK 500 3 ARG A 10 43.30 -78.55
REMARK 500 3 LEU A 12 43.26 -86.03
REMARK 500 3 CYS A 48 -91.05 -86.49
REMARK 500 3 ASP A 49 -157.25 -173.23
REMARK 500 3 GLU A 50 -89.61 -86.27
REMARK 500 3 HIS A 51 -54.26 -149.88
REMARK 500 4 GLN A 2 -81.31 -176.81
REMARK 500 4 ARG A 10 43.15 -84.89
REMARK 500 4 LEU A 12 43.54 -80.18
REMARK 500 4 ASP A 19 42.14 -84.71
REMARK 500 4 CYS A 31 -71.44 -51.40
REMARK 500 4 HIS A 51 -47.42 -151.85
REMARK 500 4 HIS A 53 38.37 -145.50
REMARK 500 5 GLN A 2 -68.31 -175.96
REMARK 500 5 ARG A 10 47.51 -70.36
REMARK 500 5 LEU A 12 42.44 -77.55
REMARK 500 5 ASN A 21 92.62 -68.68
REMARK 500 5 HIS A 44 -171.52 -179.39
REMARK 500 5 GLU A 50 88.13 -154.14
REMARK 500 5 HIS A 51 83.43 -161.06
REMARK 500 5 HIS A 53 47.06 -104.28
REMARK 500 6 GLN A 2 -54.90 -176.22
REMARK 500 6 ASN A 4 -55.87 -176.62
REMARK 500 6 GLU A 7 34.41 176.57
REMARK 500 6 ARG A 10 44.26 -77.01
REMARK 500 6 ARG A 14 100.37 -46.20
REMARK 500 6 SER A 24 -37.48 -37.17
REMARK 500 6 LEU A 29 -70.03 -51.26
REMARK 500 6 CYS A 31 -72.18 -51.49
REMARK 500 6 GLU A 35 -78.33 -75.31
REMARK 500
REMARK 500 THIS ENTRY HAS 145 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 PHE A 1 GLN A 2 3 141.39
REMARK 500 PHE A 1 GLN A 2 4 140.89
REMARK 500 PHE A 1 GLN A 2 7 139.35
REMARK 500 PHE A 1 GLN A 2 12 145.23
REMARK 500 PHE A 1 GLN A 2 15 140.91
REMARK 500 PHE A 1 GLN A 2 17 143.32
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 2 ARG A 14 0.08 SIDE CHAIN
REMARK 500 12 ARG A 14 0.09 SIDE CHAIN
REMARK 500 12 TYR A 23 0.10 SIDE CHAIN
REMARK 500 13 TYR A 23 0.07 SIDE CHAIN
REMARK 500 16 TYR A 23 0.08 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1KMA A 1 55 UNP O96790 DPGN_DIPMA 125 179
SEQRES 1 A 55 PHE GLN GLY ASN PRO CYS GLU CYS PRO ARG ALA LEU HIS
SEQRES 2 A 55 ARG VAL CYS GLY SER ASP GLY ASN THR TYR SER ASN PRO
SEQRES 3 A 55 CYS MET LEU THR CYS ALA LYS HIS GLU GLY ASN PRO ASP
SEQRES 4 A 55 LEU VAL GLN VAL HIS GLU GLY PRO CYS ASP GLU HIS ASP
SEQRES 5 A 55 HIS ASP PHE
HELIX 1 1 ASN A 25 ASN A 37 1 13
SHEET 1 A 2 VAL A 15 CYS A 16 0
SHEET 2 A 2 THR A 22 TYR A 23 -1 O TYR A 23 N VAL A 15
SSBOND 1 CYS A 6 CYS A 31 1555 1555 2.03
SSBOND 2 CYS A 8 CYS A 27 1555 1555 2.02
SSBOND 3 CYS A 16 CYS A 48 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