Header list of 1fsb.pdb file
Complete list - 29 20 Bytes
HEADER CELL ADHESION PROTEIN 25-MAR-96 1FSB
TITLE STRUCTURE OF THE EGF DOMAIN OF P-SELECTIN, NMR, 19 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: P-SELECTIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: EGF DOMAIN, RESIDUES 119 - 158;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606
KEYWDS EGF-LIKE DOMAIN, CELL ADHESION PROTEIN, TRANSMEMBRANE, GLYCOPROTEIN
EXPDTA SOLUTION NMR
NUMMDL 19
AUTHOR S.J.FREEDMAN,D.G.SANFORD,W.W.BACHOVCHIN,B.C.FURIE,J.D.BALEJA,B.FURIE
REVDAT 3 29-NOV-17 1FSB 1 REMARK HELIX
REVDAT 2 24-FEB-09 1FSB 1 VERSN
REVDAT 1 01-APR-97 1FSB 0
JRNL AUTH S.J.FREEDMAN,D.G.SANFORD,W.W.BACHOVCHIN,B.C.FURIE,
JRNL AUTH 2 J.D.BALEJA,B.FURIE
JRNL TITL STRUCTURE AND FUNCTION OF THE EPIDERMAL GROWTH FACTOR DOMAIN
JRNL TITL 2 OF P-SELECTIN.
JRNL REF BIOCHEMISTRY V. 35 13733 1996
JRNL REFN ISSN 0006-2960
JRNL PMID 8901515
JRNL DOI 10.1021/BI9610257
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NULL
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1FSB COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000173400.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 19
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 19
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
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: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 1 GLU A 14 CD GLU A 14 OE2 0.110
REMARK 500 1 GLU A 17 CD GLU A 17 OE1 0.111
REMARK 500 1 GLU A 34 CD GLU A 34 OE2 0.110
REMARK 500 1 GLU A 36 CD GLU A 36 OE1 0.110
REMARK 500 1 GLU A 40 CD GLU A 40 OE2 0.110
REMARK 500 2 GLU A 14 CD GLU A 14 OE1 0.110
REMARK 500 2 GLU A 17 CD GLU A 17 OE1 0.110
REMARK 500 2 GLU A 34 CD GLU A 34 OE1 0.110
REMARK 500 2 GLU A 36 CD GLU A 36 OE2 0.110
REMARK 500 2 GLU A 40 CD GLU A 40 OE1 0.109
REMARK 500 3 GLU A 14 CD GLU A 14 OE1 0.110
REMARK 500 3 GLU A 17 CD GLU A 17 OE1 0.114
REMARK 500 3 GLU A 34 CD GLU A 34 OE2 0.110
REMARK 500 3 GLU A 36 CD GLU A 36 OE1 0.110
REMARK 500 3 GLU A 40 CD GLU A 40 OE2 0.110
REMARK 500 4 GLU A 14 CD GLU A 14 OE1 0.110
REMARK 500 4 GLU A 17 CD GLU A 17 OE2 0.110
REMARK 500 4 GLU A 34 CD GLU A 34 OE1 0.109
REMARK 500 4 GLU A 36 CD GLU A 36 OE2 0.110
REMARK 500 4 GLU A 40 CD GLU A 40 OE2 0.109
REMARK 500 5 GLU A 14 CD GLU A 14 OE2 0.110
REMARK 500 5 GLU A 17 CD GLU A 17 OE1 0.110
REMARK 500 5 GLU A 34 CD GLU A 34 OE1 0.110
REMARK 500 5 GLU A 36 CD GLU A 36 OE1 0.110
REMARK 500 5 GLU A 40 CD GLU A 40 OE1 0.110
REMARK 500 6 GLU A 14 CD GLU A 14 OE1 0.110
REMARK 500 6 GLU A 17 CD GLU A 17 OE2 0.110
REMARK 500 6 GLU A 34 CD GLU A 34 OE2 0.109
REMARK 500 6 GLU A 36 CD GLU A 36 OE1 0.111
REMARK 500 6 GLU A 40 CD GLU A 40 OE1 0.110
REMARK 500 7 GLU A 14 CD GLU A 14 OE2 0.110
REMARK 500 7 GLU A 17 CD GLU A 17 OE2 0.110
REMARK 500 7 GLU A 34 CD GLU A 34 OE1 0.111
REMARK 500 7 GLU A 36 CD GLU A 36 OE1 0.110
REMARK 500 7 GLU A 40 CD GLU A 40 OE1 0.111
REMARK 500 8 GLU A 14 CD GLU A 14 OE2 0.110
REMARK 500 8 GLU A 17 CD GLU A 17 OE1 0.111
REMARK 500 8 GLU A 34 CD GLU A 34 OE1 0.111
REMARK 500 8 GLU A 36 CD GLU A 36 OE2 0.110
REMARK 500 8 GLU A 40 CD GLU A 40 OE2 0.110
REMARK 500 9 GLU A 14 CD GLU A 14 OE1 0.110
REMARK 500 9 GLU A 17 CD GLU A 17 OE2 0.110
REMARK 500 9 GLU A 34 CD GLU A 34 OE1 0.109
REMARK 500 9 GLU A 36 CD GLU A 36 OE2 0.111
REMARK 500 9 GLU A 40 CD GLU A 40 OE1 0.110
REMARK 500 10 GLU A 14 CD GLU A 14 OE2 0.110
REMARK 500 10 GLU A 17 CD GLU A 17 OE2 0.110
REMARK 500 10 GLU A 34 CD GLU A 34 OE1 0.110
REMARK 500 10 GLU A 36 CD GLU A 36 OE2 0.109
REMARK 500 10 GLU A 40 CD GLU A 40 OE2 0.110
REMARK 500
REMARK 500 THIS ENTRY HAS 95 BOND DEVIATIONS.
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 1 ARG A 39 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 2 ASP A 6 CB - CG - OD1 ANGL. DEV. = -5.5 DEGREES
REMARK 500 2 ARG A 39 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 3 ASP A 6 CB - CG - OD2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 3 ARG A 39 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 4 ASP A 6 CB - CG - OD1 ANGL. DEV. = -5.7 DEGREES
REMARK 500 4 TYR A 22 CA - CB - CG ANGL. DEV. = 14.7 DEGREES
REMARK 500 4 ARG A 39 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 5 ASP A 6 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 5 ARG A 39 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 6 ARG A 39 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 7 ASP A 6 CB - CG - OD1 ANGL. DEV. = -5.5 DEGREES
REMARK 500 7 ARG A 39 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 8 ASP A 6 CB - CG - OD2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 8 ARG A 39 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 9 ASP A 6 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 9 ARG A 39 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 10 ASP A 6 CB - CG - OD1 ANGL. DEV. = -5.5 DEGREES
REMARK 500 10 ARG A 39 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 11 ASP A 6 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 11 ARG A 39 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 12 ASP A 6 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 12 ARG A 39 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 13 ASP A 6 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 13 ARG A 39 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 14 ASP A 6 CB - CG - OD1 ANGL. DEV. = -5.5 DEGREES
REMARK 500 14 ARG A 39 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 15 ASP A 6 CB - CG - OD2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 15 ARG A 39 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 16 ASP A 6 CB - CG - OD1 ANGL. DEV. = -5.5 DEGREES
REMARK 500 16 ARG A 39 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 17 ASP A 6 CB - CG - OD2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 17 ARG A 39 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 18 ASP A 6 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 18 ARG A 39 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 19 ASP A 6 CB - CG - OD2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 19 ARG A 39 NE - CZ - NH1 ANGL. DEV. = 4.2 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 ALA A 2 -163.32 -173.94
REMARK 500 1 SER A 3 106.00 -53.35
REMARK 500 1 CYS A 4 91.13 25.32
REMARK 500 1 GLN A 5 -165.44 -121.33
REMARK 500 1 MET A 7 59.89 -111.23
REMARK 500 1 SER A 8 -84.06 -42.02
REMARK 500 1 LEU A 16 77.36 -113.43
REMARK 500 1 ASN A 21 -154.93 -168.35
REMARK 500 2 SER A 3 81.29 63.22
REMARK 500 2 CYS A 4 89.86 30.25
REMARK 500 2 GLN A 5 -130.62 -106.28
REMARK 500 2 MET A 7 42.41 -103.62
REMARK 500 2 CYS A 9 75.77 40.93
REMARK 500 2 SER A 10 -96.45 46.45
REMARK 500 2 LYS A 11 32.21 -166.30
REMARK 500 2 ASN A 21 -160.59 -176.95
REMARK 500 2 SER A 25 76.34 -103.75
REMARK 500 3 SER A 3 -137.88 -125.87
REMARK 500 3 GLN A 5 -163.48 -122.69
REMARK 500 3 SER A 8 -83.69 -44.19
REMARK 500 3 ASN A 21 -167.74 178.81
REMARK 500 3 SER A 25 78.59 -109.19
REMARK 500 3 PRO A 28 107.18 -57.47
REMARK 500 4 ALA A 2 96.88 -178.04
REMARK 500 4 ASP A 6 -85.77 30.24
REMARK 500 4 SER A 8 -163.78 55.07
REMARK 500 4 THR A 18 -160.96 -120.36
REMARK 500 4 ASN A 21 143.31 170.17
REMARK 500 4 THR A 23 -165.05 -121.83
REMARK 500 4 TYR A 27 160.28 -43.63
REMARK 500 4 PRO A 28 26.08 -76.64
REMARK 500 5 SER A 3 -103.17 -138.70
REMARK 500 5 GLN A 5 -109.78 -136.75
REMARK 500 5 MET A 7 37.04 -93.49
REMARK 500 5 SER A 8 110.79 -35.01
REMARK 500 5 THR A 18 -164.00 -105.93
REMARK 500 5 ILE A 19 -90.70 -36.94
REMARK 500 5 ASN A 21 -166.64 -171.96
REMARK 500 5 PRO A 28 104.66 -52.41
REMARK 500 5 ARG A 39 -152.78 -64.67
REMARK 500 6 ALA A 2 -61.89 -177.79
REMARK 500 6 SER A 3 -139.10 -147.96
REMARK 500 6 GLN A 5 -155.22 -110.58
REMARK 500 6 MET A 7 35.42 -92.00
REMARK 500 6 SER A 10 -164.85 48.92
REMARK 500 6 LYS A 11 47.45 -96.14
REMARK 500 6 ILE A 19 -93.37 -27.63
REMARK 500 6 ASN A 21 176.23 174.07
REMARK 500 6 SER A 25 78.89 -112.04
REMARK 500 6 PRO A 28 29.11 -78.52
REMARK 500
REMARK 500 THIS ENTRY HAS 155 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 4 TYR A 22 0.07 SIDE CHAIN
REMARK 500 18 TYR A 22 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1FSB A 1 40 UNP P16109 LYAM3_HUMAN 160 199
SEQRES 1 A 40 THR ALA SER CYS GLN ASP MET SER CYS SER LYS GLN GLY
SEQRES 2 A 40 GLU CYS LEU GLU THR ILE GLY ASN TYR THR CYS SER CYS
SEQRES 3 A 40 TYR PRO GLY PHE TYR GLY PRO GLU CYS GLU TYR VAL ARG
SEQRES 4 A 40 GLU
SHEET 1 S1 2 GLN A 12 THR A 18 0
SHEET 2 S1 2 ASN A 21 TYR A 27 -1
SHEET 1 S2 2 GLY A 29 GLY A 32 0
SHEET 2 S2 2 GLU A 36 ARG A 39 -1
SSBOND 1 CYS A 4 CYS A 15 1555 1555 2.04
SSBOND 2 CYS A 9 CYS A 24 1555 1555 2.04
SSBOND 3 CYS A 26 CYS A 35 1555 1555 2.05
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 - 29 20 Bytes