Header list of 1irh.pdb file
Complete list - b 23 2 Bytes
HEADER PROTEIN BINDING 02-OCT-01 1IRH
TITLE THE SOLUTION STRUCTURE OF THE THIRD KUNITZ DOMAIN OF TISSUE FACTOR
TITLE 2 PATHWAY INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TISSUE FACTOR PATHWAY INHIBITOR;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: THE THIRD KUNITZ DOMAIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: PICHIA PASTORIS;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 4922;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: GS115;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PPIC9
KEYWDS NON-PROTEASE INHIBITOR, KUNITZ DOMAIN, PROTEIN BINDING
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR S.MINE,T.YAMAZAKI,T.MIYATA,S.HARA,H.KATO
REVDAT 5 23-FEB-22 1IRH 1 REMARK
REVDAT 4 24-FEB-09 1IRH 1 VERSN
REVDAT 3 14-JAN-03 1IRH 1 REMARK
REVDAT 2 13-FEB-02 1IRH 1 COMPND
REVDAT 1 06-FEB-02 1IRH 0
JRNL AUTH S.MINE,T.YAMAZAKI,T.MIYATA,S.HARA,H.KATO
JRNL TITL STRUCTURAL MECHANISM FOR HEPARIN-BINDING OF THE THIRD KUNITZ
JRNL TITL 2 DOMAIN OF HUMAN TISSUE FACTOR PATHWAY INHIBITOR.
JRNL REF BIOCHEMISTRY V. 41 78 2002
JRNL REFN ISSN 0006-2960
JRNL PMID 11772005
JRNL DOI 10.1021/BI011299G
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1, X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER (X-PLOR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1IRH COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 04-OCT-01.
REMARK 100 THE DEPOSITION ID IS D_1000005211.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6
REMARK 210 IONIC STRENGTH : 0.1
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM THE THIRD KUNITZ DOMAIN OF
REMARK 210 TISSUE FACTOR PATHWAY INHIBITOR
REMARK 210 U-15N; 20MM NA-PHOSPHATE BUFFER;
REMARK 210 90% H2O, 10% D2O; 1MM THE THIRD
REMARK 210 KUNITZ DOMAIN OF TISSUE FACTOR
REMARK 210 PATHWAY INHIBITOR U-15N, 13C;
REMARK 210 20MM NA-PHOSPHATE BUFFER; 90%
REMARK 210 H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; HNCO-TROSY;
REMARK 210 HMQC-J; HCCH-TOCSY; HNCACB
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 40
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : ALL CALCULATED STRUCTURES
REMARK 210 SUBMITTED,BACK CALCULATED DATA
REMARK 210 AGREE WITH EXPERIMENTAL NOESY
REMARK 210 SPECTRUM,STRUCTURES WITH
REMARK 210 ACCEPTABLE COVALENT GEOMETRY,
REMARK 210 STRUCTURES WITH FAVORABLE NON-
REMARK 210 BOND ENERGY,STRUCTURES WITH THE
REMARK 210 LEAST RESTRAINT VIOLATIONS,
REMARK 210 STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY,TARGET FUNCTION
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: 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 PRO A 5 -156.34 -62.02
REMARK 500 1 SER A 6 37.00 -142.24
REMARK 500 1 TRP A 7 15.83 -155.12
REMARK 500 1 LEU A 16 -81.65 -155.75
REMARK 500 1 CYS A 17 -165.95 -73.64
REMARK 500 1 ASN A 22 74.84 -152.39
REMARK 500 1 ALA A 57 -67.83 -96.53
REMARK 500 1 LYS A 60 86.91 53.39
REMARK 500 2 HIS A 3 50.41 -162.19
REMARK 500 2 SER A 6 36.45 -97.89
REMARK 500 2 TRP A 7 24.01 -155.89
REMARK 500 2 ALA A 12 97.53 -63.10
REMARK 500 2 ARG A 14 72.31 -153.06
REMARK 500 2 ARG A 18 54.04 -101.34
REMARK 500 2 GLU A 21 -153.53 -80.62
REMARK 500 2 ASN A 22 67.03 -160.29
REMARK 500 2 ASN A 44 -154.90 -89.69
REMARK 500 3 LEU A 16 -44.39 -160.05
REMARK 500 3 CYS A 41 27.94 -151.75
REMARK 500 3 ALA A 57 -66.12 -98.89
REMARK 500 3 LYS A 60 79.34 57.45
REMARK 500 4 HIS A 3 176.65 55.26
REMARK 500 4 PRO A 5 -155.10 -61.93
REMARK 500 4 TRP A 7 15.85 -150.18
REMARK 500 4 LEU A 16 -85.07 56.99
REMARK 500 4 CYS A 17 -161.75 -119.01
REMARK 500 4 ARG A 18 103.98 -58.87
REMARK 500 4 ASN A 22 70.81 -157.09
REMARK 500 4 LYS A 37 93.69 -68.92
REMARK 500 4 SER A 39 -172.20 -62.68
REMARK 500 4 CYS A 41 -72.88 -145.35
REMARK 500 4 ASN A 44 -159.66 -78.23
REMARK 500 5 PHE A 2 98.45 53.92
REMARK 500 5 PRO A 5 -164.46 -60.69
REMARK 500 5 SER A 6 37.63 -154.83
REMARK 500 5 PRO A 11 -173.38 -63.49
REMARK 500 5 CYS A 17 179.58 54.57
REMARK 500 5 ALA A 19 149.72 -174.33
REMARK 500 5 GLU A 21 -158.62 -89.31
REMARK 500 5 ASN A 22 88.42 -160.95
REMARK 500 5 LYS A 60 71.92 50.87
REMARK 500 6 HIS A 3 -56.11 -127.96
REMARK 500 6 PRO A 5 -174.79 -60.83
REMARK 500 6 LEU A 16 -44.47 -139.22
REMARK 500 6 GLU A 21 -161.96 -79.75
REMARK 500 7 PHE A 2 35.53 -141.31
REMARK 500 7 PRO A 5 -169.48 -59.67
REMARK 500 7 TRP A 7 13.95 -146.71
REMARK 500 7 ALA A 12 104.11 -58.60
REMARK 500 7 CYS A 17 -157.78 -157.15
REMARK 500
REMARK 500 THIS ENTRY HAS 160 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 14 0.22 SIDE CHAIN
REMARK 500 1 ARG A 18 0.27 SIDE CHAIN
REMARK 500 1 ARG A 23 0.28 SIDE CHAIN
REMARK 500 1 ARG A 34 0.31 SIDE CHAIN
REMARK 500 1 ARG A 56 0.26 SIDE CHAIN
REMARK 500 2 ARG A 14 0.30 SIDE CHAIN
REMARK 500 2 ARG A 18 0.30 SIDE CHAIN
REMARK 500 2 ARG A 23 0.23 SIDE CHAIN
REMARK 500 2 ARG A 34 0.29 SIDE CHAIN
REMARK 500 2 ARG A 56 0.32 SIDE CHAIN
REMARK 500 3 ARG A 14 0.31 SIDE CHAIN
REMARK 500 3 ARG A 18 0.32 SIDE CHAIN
REMARK 500 3 ARG A 23 0.24 SIDE CHAIN
REMARK 500 3 ARG A 34 0.31 SIDE CHAIN
REMARK 500 3 ARG A 56 0.21 SIDE CHAIN
REMARK 500 4 ARG A 14 0.28 SIDE CHAIN
REMARK 500 4 ARG A 18 0.29 SIDE CHAIN
REMARK 500 4 ARG A 23 0.28 SIDE CHAIN
REMARK 500 4 ARG A 34 0.31 SIDE CHAIN
REMARK 500 4 ARG A 56 0.25 SIDE CHAIN
REMARK 500 5 ARG A 14 0.28 SIDE CHAIN
REMARK 500 5 ARG A 18 0.29 SIDE CHAIN
REMARK 500 5 ARG A 23 0.23 SIDE CHAIN
REMARK 500 5 ARG A 34 0.31 SIDE CHAIN
REMARK 500 5 ARG A 56 0.23 SIDE CHAIN
REMARK 500 6 ARG A 14 0.32 SIDE CHAIN
REMARK 500 6 ARG A 18 0.23 SIDE CHAIN
REMARK 500 6 ARG A 23 0.21 SIDE CHAIN
REMARK 500 6 ARG A 34 0.28 SIDE CHAIN
REMARK 500 6 ARG A 56 0.28 SIDE CHAIN
REMARK 500 7 ARG A 14 0.31 SIDE CHAIN
REMARK 500 7 ARG A 18 0.28 SIDE CHAIN
REMARK 500 7 ARG A 23 0.30 SIDE CHAIN
REMARK 500 7 ARG A 34 0.32 SIDE CHAIN
REMARK 500 7 ARG A 56 0.29 SIDE CHAIN
REMARK 500 8 ARG A 14 0.21 SIDE CHAIN
REMARK 500 8 ARG A 18 0.30 SIDE CHAIN
REMARK 500 8 ARG A 23 0.31 SIDE CHAIN
REMARK 500 8 ARG A 34 0.24 SIDE CHAIN
REMARK 500 8 ARG A 56 0.30 SIDE CHAIN
REMARK 500 9 ARG A 14 0.31 SIDE CHAIN
REMARK 500 9 ARG A 18 0.31 SIDE CHAIN
REMARK 500 9 ARG A 23 0.22 SIDE CHAIN
REMARK 500 9 ARG A 34 0.20 SIDE CHAIN
REMARK 500 9 ARG A 56 0.31 SIDE CHAIN
REMARK 500 10 ARG A 14 0.20 SIDE CHAIN
REMARK 500 10 ARG A 18 0.29 SIDE CHAIN
REMARK 500 10 ARG A 23 0.26 SIDE CHAIN
REMARK 500 10 ARG A 34 0.30 SIDE CHAIN
REMARK 500 10 ARG A 56 0.32 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 100 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1IRH A 1 61 UNP P10646 TFPI1_HUMAN 210 270
SEQRES 1 A 61 GLU PHE HIS GLY PRO SER TRP CYS LEU THR PRO ALA ASP
SEQRES 2 A 61 ARG GLY LEU CYS ARG ALA ASN GLU ASN ARG PHE TYR TYR
SEQRES 3 A 61 ASN SER VAL ILE GLY LYS CYS ARG PRO PHE LYS TYR SER
SEQRES 4 A 61 GLY CYS GLY GLY ASN GLU ASN ASN PHE THR SER LYS GLN
SEQRES 5 A 61 GLU CYS LEU ARG ALA CYS LYS LYS GLY
HELIX 1 1 LYS A 51 LYS A 59 1 9
SHEET 1 A 2 ARG A 23 TYR A 26 0
SHEET 2 A 2 CYS A 33 PHE A 36 -1 O PHE A 36 N ARG A 23
SSBOND 1 CYS A 8 CYS A 58 1555 1555 2.03
SSBOND 2 CYS A 17 CYS A 41 1555 1555 2.02
SSBOND 3 CYS A 33 CYS A 54 1555 1555 2.02
CRYST1 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