Header list of 1itp.pdb file
Complete list - b 23 2 Bytes
HEADER PROTEIN BINDING 23-JAN-02 1ITP
TITLE SOLUTION STRUCTURE OF POIA1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEINASE A INHIBITOR 1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: IA-1=SERINE PROTEINASE INHIBITOR;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PLEUROTUS OSTREATUS;
SOURCE 3 ORGANISM_COMMON: OYSTER MUSHROOM;
SOURCE 4 ORGANISM_TAXID: 5322;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET11D
KEYWDS INHIBITOR, PROPEPTIDE, BETA-ALPHA-BETA, PROTEIN BINDING
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR H.SASAKAWA,S.YOSHINAGA,S.KOJIMA,A.TAMURA
REVDAT 5 23-FEB-22 1ITP 1 REMARK SEQADV
REVDAT 4 24-FEB-09 1ITP 1 VERSN
REVDAT 3 07-JAN-03 1ITP 1 REMARK
REVDAT 2 10-APR-02 1ITP 1 JRNL
REVDAT 1 13-FEB-02 1ITP 0
JRNL AUTH H.SASAKAWA,S.YOSHINAGA,S.KOJIMA,A.TAMURA
JRNL TITL STRUCTURE OF POIA1, A HOMOLOGOUS PROTEIN TO THE PROPEPTIDE
JRNL TITL 2 OF SUBTILISIN: IMPLICATION FOR PROTEIN FOLDABILITY AND THE
JRNL TITL 3 FUNCTION AS AN INTRAMOLECULAR CHAPERONE.
JRNL REF J.MOL.BIOL. V. 317 159 2002
JRNL REFN ISSN 0022-2836
JRNL PMID 11916386
JRNL DOI 10.1006/JMBI.2002.5412
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA 1.5, DYANA 1.5
REMARK 3 AUTHORS : GNTERT (DYANA), GNTERT (DYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1ITP COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-JAN-02.
REMARK 100 THE DEPOSITION ID IS D_1000005264.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303; 303; 303
REMARK 210 PH : 7.0; 7.0; 7.0
REMARK 210 IONIC STRENGTH : 25MM PI; 25MM PI; 25MM PI
REMARK 210 PRESSURE : 1 ATM; 1 ATM; 1 ATM
REMARK 210 SAMPLE CONTENTS : 1MM POIA1, 25MM PHOSPHATE
REMARK 210 BUFFER, 95% H2O, 5% D2O; 1MM
REMARK 210 POIA1 U-15N, 25MM PHOSPHATE
REMARK 210 BUFFER, 95% H2O, 5% D2O; 1MM
REMARK 210 POIA1 U-15N, 13C, 25MM PHOSPHATE
REMARK 210 BUFFER, 95% H2O, 5% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; 3HJNC'-HNCO
REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ
REMARK 210 SPECTROMETER MODEL : DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 1.3, NMRPIPE 1.7
REMARK 210 METHOD USED : DISTANCE GEOMETRY
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 : 20
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 O GLU A 21 H GLU A 25 1.55
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 SER A 2 172.97 -47.41
REMARK 500 1 LYS A 11 177.13 -49.02
REMARK 500 1 ASN A 12 34.18 -93.54
REMARK 500 1 VAL A 14 153.61 -38.17
REMARK 500 1 GLU A 29 -70.28 -53.30
REMARK 500 1 ASN A 38 70.10 -106.20
REMARK 500 1 LEU A 54 -72.72 -53.05
REMARK 500 1 THR A 55 -30.76 -37.12
REMARK 500 1 LYS A 56 -71.83 -59.04
REMARK 500 1 GLN A 61 166.72 -43.22
REMARK 500 1 LEU A 64 -65.06 -160.13
REMARK 500 1 VAL A 74 -62.52 -104.99
REMARK 500 1 THR A 75 150.89 62.44
REMARK 500 1 THR A 76 90.48 44.80
REMARK 500 2 SER A 2 135.78 72.44
REMARK 500 2 LYS A 11 -178.49 -51.34
REMARK 500 2 ASN A 12 35.83 -96.61
REMARK 500 2 VAL A 14 150.74 -38.64
REMARK 500 2 LEU A 54 -74.44 -54.17
REMARK 500 2 THR A 55 -30.42 -37.79
REMARK 500 2 GLN A 61 160.99 -39.91
REMARK 500 2 LEU A 64 -70.53 -157.91
REMARK 500 2 THR A 75 87.58 44.44
REMARK 500 3 SER A 2 164.14 72.18
REMARK 500 3 LYS A 11 177.73 -49.46
REMARK 500 3 ASN A 12 34.71 -93.49
REMARK 500 3 VAL A 14 152.35 -38.94
REMARK 500 3 THR A 22 -36.91 -38.66
REMARK 500 3 LEU A 54 -76.33 -54.03
REMARK 500 3 THR A 55 -31.55 -39.94
REMARK 500 3 ASP A 63 -61.84 -123.47
REMARK 500 3 THR A 75 65.89 -159.06
REMARK 500 4 SER A 2 -139.72 -62.54
REMARK 500 4 ALA A 3 42.96 -91.19
REMARK 500 4 LYS A 11 178.79 -50.20
REMARK 500 4 ASN A 12 34.59 -94.92
REMARK 500 4 VAL A 14 152.13 -38.31
REMARK 500 4 LEU A 54 -70.82 -52.25
REMARK 500 4 THR A 55 -30.18 -37.74
REMARK 500 4 GLN A 61 148.11 -39.86
REMARK 500 4 LEU A 64 -48.30 -152.04
REMARK 500 4 GLU A 69 67.52 -112.14
REMARK 500 4 VAL A 74 78.98 -117.65
REMARK 500 4 THR A 75 143.98 63.40
REMARK 500 5 LYS A 11 -175.99 -52.01
REMARK 500 5 ASN A 12 35.75 -99.37
REMARK 500 5 VAL A 14 146.22 -39.40
REMARK 500 5 LEU A 54 -81.19 -52.46
REMARK 500 5 THR A 55 -29.99 -38.80
REMARK 500 5 GLN A 61 146.55 -39.77
REMARK 500
REMARK 500 THIS ENTRY HAS 228 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1ITP A 2 77 UNP Q7M4T6 PIA1_PLEOS 1 76
SEQADV 1ITP GLY A 1 UNP Q7M4T6 CLONING ARTIFACT
SEQRES 1 A 77 GLY SER ALA GLY LYS PHE ILE VAL ILE PHE LYS ASN ASP
SEQRES 2 A 77 VAL SER GLU ASP LYS ILE ARG GLU THR LYS ASP GLU VAL
SEQRES 3 A 77 ILE ALA GLU GLY GLY THR ILE THR ASN GLU TYR ASN MET
SEQRES 4 A 77 PRO GLY MET LYS GLY PHE ALA GLY GLU LEU THR PRO GLN
SEQRES 5 A 77 SER LEU THR LYS PHE GLN GLY LEU GLN GLY ASP LEU ILE
SEQRES 6 A 77 ASP SER ILE GLU GLU ASP GLY ILE VAL THR THR GLN
HELIX 1 1 SER A 15 GLY A 30 1 16
HELIX 2 2 THR A 50 LEU A 60 1 11
SHEET 1 A 4 ASN A 35 MET A 39 0
SHEET 2 A 4 MET A 42 LEU A 49 -1 O ALA A 46 N ASN A 35
SHEET 3 A 4 GLY A 4 PHE A 10 -1 N PHE A 10 O LYS A 43
SHEET 4 A 4 ILE A 65 GLU A 70 -1 O GLU A 69 N ILE A 7
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