Header list of 1iw4.pdb file
Complete list - g 9 2 Bytes
HEADER PROTEIN BINDING 19-APR-02 1IW4
TITLE SOLUTION STRUCTURE OF ASCIDIAN TRYPSIN INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRYPSIN INHIBITOR;
COMPND 3 CHAIN: A
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HALOCYNTHIA RORETZI;
SOURCE 3 ORGANISM_TAXID: 7729
KEYWDS SOLUTION STRUCTURE, ASCIDIAN, TRYPSIN INHIBITOR, CYSTINE-STABILIZED
KEYWDS 2 ALPHA-HELICAL MOTIF, DISULFIDE BOND, KAZAL-TYPE INHIBITOR, PROTEIN
KEYWDS 3 BINDING
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR H.HEMMI,T.YOSHIDA,T.KUMAZAKI,N.NEMOTO,J.HASEGAWA,F.NISHIOKA,
AUTHOR 2 Y.KYOGOKU,H.YOKOSAWA,Y.KOBAYASHI
REVDAT 4 14-JUN-23 1IW4 1 REMARK
REVDAT 3 26-FEB-20 1IW4 1 REMARK
REVDAT 2 24-FEB-09 1IW4 1 VERSN
REVDAT 1 28-AUG-02 1IW4 0
JRNL AUTH H.HEMMI,T.YOSHIDA,T.KUMAZAKI,N.NEMOTO,J.HASEGAWA,F.NISHIOKA,
JRNL AUTH 2 Y.KYOGOKU,H.YOKOSAWA,Y.KOBAYASHI
JRNL TITL SOLUTION STRUCTURE OF ASCIDIAN TRYPSIN INHIBITOR DETERMINED
JRNL TITL 2 BY NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY.
JRNL REF BIOCHEMISTRY V. 41 10657 2002
JRNL REFN ISSN 0006-2960
JRNL PMID 12186551
JRNL DOI 10.1021/BI026035O
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, CNS 1.0
REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1IW4 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-APR-02.
REMARK 100 THE DEPOSITION ID IS D_1000005328.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303; 303
REMARK 210 PH : 3.7; 3.7
REMARK 210 IONIC STRENGTH : NULL; NULL
REMARK 210 PRESSURE : AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.5-2.0MM ASCIDIAN TRYPSIN
REMARK 210 INHIBITOR; 90% H2O, 10% D2O; 1.5-
REMARK 210 2.0MM ASCIDIAN TRYPSIN INHIBITOR;
REMARK 210 D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; DQF-COSY; E-COSY; TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE; DRX; DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; JEOL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 2.1, NMRPIPP 4.3.2
REMARK 210 METHOD USED : SIMULATED ANNEALING
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 : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING STANDARD 2D HOMONUCLEAR
REMARK 210 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: 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 O ASN A 15 N MET A 17 2.00
REMARK 500 O LEU A 11 N ARG A 13 2.01
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 HIS A 2 84.64 -69.58
REMARK 500 1 GLU A 7 78.05 -42.07
REMARK 500 1 PHE A 8 -147.67 -160.68
REMARK 500 1 ASN A 9 -71.28 -69.11
REMARK 500 1 LEU A 11 171.42 -47.84
REMARK 500 1 CYS A 12 62.98 -28.00
REMARK 500 1 ARG A 13 41.48 -92.38
REMARK 500 1 LYS A 16 57.49 -20.44
REMARK 500 1 MET A 17 78.58 -65.09
REMARK 500 1 LEU A 18 59.39 -170.87
REMARK 500 1 ASP A 20 178.25 -54.43
REMARK 500 1 LEU A 21 66.11 -170.35
REMARK 500 1 ASP A 28 24.22 -154.08
REMARK 500 2 HIS A 2 52.39 -114.91
REMARK 500 2 THR A 6 -116.85 -61.16
REMARK 500 2 GLU A 7 26.38 179.37
REMARK 500 2 PRO A 10 87.58 -67.06
REMARK 500 2 LEU A 11 -167.97 -47.81
REMARK 500 2 CYS A 12 60.71 -17.79
REMARK 500 2 ARG A 13 42.85 -98.22
REMARK 500 2 LYS A 16 58.21 -19.45
REMARK 500 2 LEU A 18 59.18 -162.65
REMARK 500 2 ASP A 28 23.59 -152.47
REMARK 500 2 PHE A 47 -122.87 -61.92
REMARK 500 2 CYS A 54 -73.03 -164.16
REMARK 500 3 HIS A 2 72.48 -69.83
REMARK 500 3 MET A 3 103.49 -170.87
REMARK 500 3 ASP A 4 30.79 179.54
REMARK 500 3 THR A 6 -124.33 -62.14
REMARK 500 3 GLU A 7 24.56 179.13
REMARK 500 3 PRO A 10 71.85 -66.92
REMARK 500 3 LEU A 11 -170.62 -54.78
REMARK 500 3 CYS A 12 65.85 -17.97
REMARK 500 3 ARG A 13 30.69 -80.37
REMARK 500 3 ASN A 15 -53.40 -160.71
REMARK 500 3 LYS A 16 57.75 -19.71
REMARK 500 3 LEU A 18 63.25 -171.18
REMARK 500 3 ASP A 28 24.28 -154.91
REMARK 500 3 PHE A 47 167.21 -48.82
REMARK 500 3 CYS A 54 -36.66 177.06
REMARK 500 4 MET A 3 -62.46 -171.85
REMARK 500 4 ASP A 4 118.10 -23.70
REMARK 500 4 CYS A 5 -159.70 -160.67
REMARK 500 4 GLU A 7 89.81 -34.63
REMARK 500 4 PHE A 8 -155.80 -160.02
REMARK 500 4 LEU A 11 179.59 -57.03
REMARK 500 4 CYS A 12 63.18 -37.18
REMARK 500 4 ARG A 13 41.53 -91.88
REMARK 500 4 ASN A 15 -73.45 -104.09
REMARK 500 4 MET A 17 142.15 -19.75
REMARK 500
REMARK 500 THIS ENTRY HAS 292 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5348 RELATED DB: BMRB
REMARK 900 5348 IS CHEMICAL SHIFTS OF THIS PROTEIN
DBREF 1IW4 A 1 55 UNP P16589 ITRP_HALRO 1 55
SEQRES 1 A 55 ALA HIS MET ASP CYS THR GLU PHE ASN PRO LEU CYS ARG
SEQRES 2 A 55 CYS ASN LYS MET LEU GLY ASP LEU ILE CYS ALA VAL ILE
SEQRES 3 A 55 GLY ASP ALA LYS GLU GLU HIS ARG ASN MET CYS ALA LEU
SEQRES 4 A 55 CYS CYS GLU HIS PRO GLY GLY PHE GLU TYR SER ASN GLY
SEQRES 5 A 55 PRO CYS GLU
HELIX 1 1 ASN A 35 HIS A 43 1 9
SHEET 1 A 3 GLU A 31 HIS A 33 0
SHEET 2 A 3 ILE A 22 VAL A 25 -1 N ALA A 24 O GLU A 31
SHEET 3 A 3 GLU A 48 TYR A 49 -1 O GLU A 48 N VAL A 25
SSBOND 1 CYS A 5 CYS A 40 1555 1555 2.03
SSBOND 2 CYS A 12 CYS A 41 1555 1555 2.02
SSBOND 3 CYS A 14 CYS A 37 1555 1555 2.03
SSBOND 4 CYS A 23 CYS A 54 1555 1555 2.03
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 - g 9 2 Bytes