Header list of 1hi7.pdb file
Complete list - r 10 2 Bytes
HEADER GROWTH FACTOR 03-JAN-01 1HI7
TITLE NMR SOLUTION STRUCTURE OF THE DISULPHIDE-LINKED HOMODIMER OF HUMAN
TITLE 2 TFF1, 10 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PS2 PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: PNR-2, PS2, TFF1, BREAST CANCER ESTROGEN INDUCIBLE PROTEIN,
COMPND 5 TREFOIL FACTOR FAMILY 1 PROTEIN;
COMPND 6 ENGINEERED: YES;
COMPND 7 OTHER_DETAILS: DISULPHIDE LINK BETWEEN C58 OF BOTH SUBUNITS
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 ORGAN: BREAST, STOMACH;
SOURCE 6 TISSUE: EPITHELIAL;
SOURCE 7 CELL: MCF-7, UACL;
SOURCE 8 CELLULAR_LOCATION: EXTRACELLULAR;
SOURCE 9 GENE: TFF1;
SOURCE 10 EXPRESSION_SYSTEM: ESCHERICHIA COLI HB101;
SOURCE 11 EXPRESSION_SYSTEM_TAXID: 634468;
SOURCE 12 EXPRESSION_SYSTEM_CELLULAR_LOCATION: CYTOPLASM;
SOURCE 13 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 14 EXPRESSION_SYSTEM_VECTOR: PHARMACIA PEZZ18;
SOURCE 15 EXPRESSION_SYSTEM_GENE: TFF1
KEYWDS GROWTH FACTOR, CELL MOTILITY, TUMOR SUPPRESSOR, TREFOIL DOMAIN
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR M.A.WILLIAMS,J.FEENEY
REVDAT 5 10-APR-19 1HI7 1 SOURCE
REVDAT 4 14-JUN-17 1HI7 1 REMARK
REVDAT 3 24-FEB-09 1HI7 1 VERSN
REVDAT 2 09-APR-01 1HI7 1 JRNL
REVDAT 1 03-JAN-01 1HI7 0
JRNL AUTH M.A.WILLIAMS,B.R.WESTLEY,F.E.MAY,J.FEENEY
JRNL TITL THE SOLUTION STRUCTURE OF THE DISULPHIDE-LINKED DIMERIC OF
JRNL TITL 2 THE HUMAN TREFOIL PROTEIN TFF1
JRNL REF FEBS LETT. V. 493 70 2001
JRNL REFN ISSN 0014-5793
JRNL PMID 11286998
JRNL DOI 10.1016/S0014-5793(01)02276-1
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH V.I.POLSHAKOV,M.A.WILLIAMS,A.R.GARGARO,T.A.FRENKIEL,
REMARK 1 AUTH 2 B.R.WESTLEY,M.P.CHADWICK,F.E.B.MAY,J.FEENEY
REMARK 1 TITL HIGH-RESOLUTION SOLUTION STRUCTURE OF HUMAN PNR-2/ PS2: A
REMARK 1 TITL 2 SINGLE TREFOIL MOTIF PROTEIN
REMARK 1 REF J.MOL.BIOL. V. 267 418 1997
REMARK 1 REFN ISSN 0022-2836
REMARK 1 PMID 9096235
REMARK 1 DOI 10.1006/JMBI.1997.0896
REMARK 1 REFERENCE 2
REMARK 1 AUTH M.P.CHADWICK,F.E.B.MAY,B.R.WESTLEY
REMARK 1 TITL HOMODIMERIZATION AND HETERO_OLIGOMERIZATION OF THE SINGLE
REMARK 1 TITL 2 DOMAIN TREFOIL PROTEIN PNR-2/PS2 THROUGH CYSTEINE 58
REMARK 1 REF BIOCHEM.J. V. 327 117 1997
REMARK 1 REFN ISSN 0264-6021
REMARK 1 PMID 9355742
REMARK 1 REFERENCE 3
REMARK 1 AUTH M.P.CHADWICK,F.E.B.MAY,B.R.WESTLEY
REMARK 1 TITL PRODUCTION AND COMPARISON OF MATURE SINGLE-DOMAIN 'TREFOIL'
REMARK 1 TITL 2 PEPTIDES PNR-2/PS2 CYS58 AND PNR-2/PS2 SER58
REMARK 1 REF BIOCHEM.J. V. 308 1001 1995
REMARK 1 REFN ISSN 0264-6021
REMARK 1 PMID 8948462
REMARK 1 REFERENCE 4
REMARK 1 AUTH V.I.POLSHAKOV,T.A.FRENKIEL,B.WESTLEY,M.CHADWICK,F.MAY,
REMARK 1 AUTH 2 M.D.CARR,J.FEENEY
REMARK 1 TITL NMR-BASED STRUCTURAL STUDIES OF THE PNR-2/PS2 SINGLE DOMAIN
REMARK 1 TITL 2 TREFOIL PEPTIDE. SIMILARITIES TO PORCINE SPASMOLYTIC PEPTIDE
REMARK 1 TITL 3 AND EVIDENCE FOR A MONOMERIC STRUCTURE
REMARK 1 REF EUR.J.BIOCHEM. V. 233 847 1995
REMARK 1 REFN ISSN 0014-2956
REMARK 1 PMID 8521850
REMARK 1 DOI 10.1111/J.1432-1033.1995.847_3.X
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN THE
REMARK 3 JRNL CITATION ABOVE
REMARK 4
REMARK 4 1HI7 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-JAN-01.
REMARK 100 THE DEPOSITION ID IS D_1290005750.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 5.9
REMARK 210 IONIC STRENGTH : 0.01
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2-D 1H-1H HOMONUCLEAR TOCSY;
REMARK 210 ROESY; NOESY; 1H/15N HSQC; HSQC-
REMARK 210 NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : UNITY; UNITYPLUS
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CNS 1.0
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 11
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : TOTAL NOE CONSTRAINT VIOLATIONS
REMARK 210 < 1.0 A
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 6
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TWO AND THREE
REMARK 210 DIMENSIONAL NMR EXPERIMENTS ON, RESPECTIVELY, UNLABELLED AND N-
REMARK 210 15 LABELLED TFF1 DIMER PROTEIN. MANY ASSIGN WERE MADE BY MAKING
REMARK 210 USE IF THE BETTER RESOLVED MONOMER SPECTRA (POLSHAKOV ET AL.
REMARK 210 1995,1997)
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 HG1 THR B 4 HB ILE B 50 1.25
REMARK 500 HB THR B 23 HD2 PRO B 24 1.27
REMARK 500 HG23 THR B 6 H CYS B 7 1.28
REMARK 500 HB2 PRO B 53 HD2 PRO B 54 1.30
REMARK 500 HG23 THR A 6 H THR A 8 1.32
REMARK 500 HA THR B 6 OG1 THR B 49 1.53
REMARK 500 HG1 THR B 4 O ILE B 50 1.59
REMARK 500 O GLU B 5 HG22 THR B 49 1.59
REMARK 500 O THR B 6 ND2 ASN B 48 2.02
REMARK 500 OG1 THR B 4 O ILE B 50 2.12
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 PHE A 19 163.88 -44.88
REMARK 500 1 PRO A 47 -161.63 -71.68
REMARK 500 1 GLU A 55 -19.77 -169.95
REMARK 500 1 GLU A 56 -29.52 -165.66
REMARK 500 1 GLU A 57 -139.64 -150.78
REMARK 500 1 ALA B 2 -132.84 -115.48
REMARK 500 1 THR B 4 -158.42 -138.34
REMARK 500 1 GLU B 5 -174.23 -48.30
REMARK 500 1 ASN B 16 150.04 -35.38
REMARK 500 1 ASP B 35 79.94 -170.20
REMARK 500 1 ASP B 36 30.41 -90.02
REMARK 500 1 ASN B 48 78.52 -150.24
REMARK 500 1 PRO B 53 -169.17 -69.80
REMARK 500 1 GLU B 57 -123.45 -132.56
REMARK 500 2 ALA A 2 -128.51 -106.10
REMARK 500 2 ASN A 16 148.85 -24.98
REMARK 500 2 VAL A 22 163.24 -39.90
REMARK 500 2 ASP A 36 54.71 -91.74
REMARK 500 2 PRO A 47 -156.78 -71.35
REMARK 500 2 ASP A 51 112.46 -164.30
REMARK 500 2 PRO A 54 -84.08 -74.80
REMARK 500 2 GLU A 57 -123.50 -101.75
REMARK 500 2 CYS A 58 -70.31 -114.39
REMARK 500 2 GLU A 59 -110.25 -95.36
REMARK 500 2 ALA B 2 -152.25 -127.75
REMARK 500 2 PHE B 19 166.71 -45.02
REMARK 500 2 ASP B 36 46.16 -96.81
REMARK 500 2 PRO B 54 -135.77 -70.01
REMARK 500 2 GLU B 55 -43.11 -150.32
REMARK 500 2 GLU B 56 -69.76 -121.70
REMARK 500 2 CYS B 58 43.62 -83.23
REMARK 500 2 GLU B 59 111.63 -160.30
REMARK 500 3 ALA A 2 70.76 -107.68
REMARK 500 3 ASN A 16 150.37 -27.63
REMARK 500 3 VAL A 22 154.68 -31.56
REMARK 500 3 ASP A 36 38.02 -89.62
REMARK 500 3 VAL A 52 30.51 -156.71
REMARK 500 3 GLU A 55 -157.41 -93.14
REMARK 500 3 GLU A 56 -20.18 -165.50
REMARK 500 3 GLU A 59 16.66 -145.08
REMARK 500 3 ALA B 2 37.24 -96.62
REMARK 500 3 THR B 8 55.73 -97.77
REMARK 500 3 ASN B 16 150.03 -33.80
REMARK 500 3 VAL B 22 158.83 -47.94
REMARK 500 3 ASP B 36 46.79 -94.78
REMARK 500 3 PRO B 47 -172.42 -69.95
REMARK 500 3 THR B 49 80.54 -67.66
REMARK 500 3 GLU B 57 60.81 -114.97
REMARK 500 3 CYS B 58 32.24 -165.57
REMARK 500 4 THR A 8 63.58 -100.30
REMARK 500
REMARK 500 THIS ENTRY HAS 155 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1PS2 RELATED DB: PDB
REMARK 900 HIGH RESOLUTION NMR SOLUTION STRUCTURE OF HUMAN PS2, 19 STRUCTURES
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 1PS2 SWS P04155 1 - 24 NOT IN ATOMS LIST
DBREF 1HI7 A 1 60 UNP P04155 PS2_HUMAN 25 84
DBREF 1HI7 B 1 60 UNP P04155 PS2_HUMAN 25 84
SEQRES 1 A 60 GLU ALA GLN THR GLU THR CYS THR VAL ALA PRO ARG GLU
SEQRES 2 A 60 ARG GLN ASN CYS GLY PHE PRO GLY VAL THR PRO SER GLN
SEQRES 3 A 60 CYS ALA ASN LYS GLY CYS CYS PHE ASP ASP THR VAL ARG
SEQRES 4 A 60 GLY VAL PRO TRP CYS PHE TYR PRO ASN THR ILE ASP VAL
SEQRES 5 A 60 PRO PRO GLU GLU GLU CYS GLU PHE
SEQRES 1 B 60 GLU ALA GLN THR GLU THR CYS THR VAL ALA PRO ARG GLU
SEQRES 2 B 60 ARG GLN ASN CYS GLY PHE PRO GLY VAL THR PRO SER GLN
SEQRES 3 B 60 CYS ALA ASN LYS GLY CYS CYS PHE ASP ASP THR VAL ARG
SEQRES 4 B 60 GLY VAL PRO TRP CYS PHE TYR PRO ASN THR ILE ASP VAL
SEQRES 5 B 60 PRO PRO GLU GLU GLU CYS GLU PHE
HELIX 1 1 THR A 23 LYS A 30 1 8
HELIX 2 2 THR B 23 LYS B 30 1 8
SHEET 1 A 2 THR A 4 THR A 6 0
SHEET 2 A 2 ASN A 48 ILE A 50 -1 O ASN A 48 N THR A 6
SHEET 1 B 2 CYS A 33 PHE A 34 0
SHEET 2 B 2 CYS A 44 PHE A 45 -1 O PHE A 45 N CYS A 33
SHEET 1 C 2 THR B 4 THR B 6 0
SHEET 2 C 2 ASN B 48 ILE B 50 -1 O ASN B 48 N THR B 6
SHEET 1 D 2 CYS B 33 PHE B 34 0
SHEET 2 D 2 CYS B 44 PHE B 45 -1 O PHE B 45 N CYS B 33
SSBOND 1 CYS A 7 CYS A 33 1555 1555 2.03
SSBOND 2 CYS A 17 CYS A 32 1555 1555 2.03
SSBOND 3 CYS A 27 CYS A 44 1555 1555 2.03
SSBOND 4 CYS A 58 CYS B 58 1555 1555 2.03
SSBOND 5 CYS B 7 CYS B 33 1555 1555 2.03
SSBOND 6 CYS B 17 CYS B 32 1555 1555 2.03
SSBOND 7 CYS B 27 CYS B 44 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 - r 10 2 Bytes