Header list of 1j8k.pdb file
Complete list - b 23 2 Bytes
HEADER PROTEIN BINDING 22-MAY-01 1J8K
TITLE NMR STRUCTURE OF THE FIBRONECTIN EDA DOMAIN, NMR, 20 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FIBRONECTIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: EXTRA DOMAIN 2 (RESIDUES 1631-1724);
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: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET28
KEYWDS EDA, FIBRONECTIN, TYPEIII DOMAIN, PROTEIN BINDING
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR T.NIIMI,M.OSAWA,N.YAMAJI,K.YASUNAGA,H.SAKASHITA,T.MASE,A.TANAKA,
AUTHOR 2 S.FUJITA
REVDAT 4 23-FEB-22 1J8K 1 REMARK
REVDAT 3 24-FEB-09 1J8K 1 VERSN
REVDAT 2 25-DEC-02 1J8K 1 REMARK
REVDAT 1 06-FEB-02 1J8K 0
JRNL AUTH T.NIIMI,M.OSAWA,N.YAMAJI,K.YASUNAGA,H.SAKASHITA,T.MASE,
JRNL AUTH 2 A.TANAKA,S.FUJITA
JRNL TITL NMR STRUCTURE OF HUMAN FIBRONECTIN EDA.
JRNL REF J.BIOMOL.NMR V. 21 281 2001
JRNL REFN ISSN 0925-2738
JRNL PMID 11775745
JRNL DOI 10.1023/A:1012947209393
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE 1998, X-PLOR 3.1
REMARK 3 AUTHORS : DELAGLIO (NMRPIPE), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THESE STRUCTURES CONSIST OF 1289 UPPER
REMARK 3 LIMITS ON DISTANCES OBTAINED FROM NOE MEASUREMENTS AND HTDROGEN
REMARK 3 EXCHANGE MEASUREMENTS AND 51 TORSION ANGLE CONSTRAINTS OBTAINED
REMARK 3 FROM COUPLING CONSTANT AND CHEMICAL SHIFT INDEX
REMARK 4
REMARK 4 1J8K COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-MAY-01.
REMARK 100 THE DEPOSITION ID IS D_1000013494.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 400MM SODIUM SULFATE
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 2MM EDA U-15N,13C; 50MM
REMARK 210 PHOSPHATE BUFFER, 400MM SODIUM
REMARK 210 SULFATE; 90% H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; HNHA
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR 3.1
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THREE-DIMENSIONAL STRUCTURE IN SOLUTION REPRESENTED BY 20
REMARK 210 CONFORMERS DETERMINED BY NUCLEAR MAGNETIC RESONANCE, TORSION
REMARK 210 ANGLE DYNAMICS AND RESTRAINED ENERGY REFINEMENT.
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 HIS A 76 H ASP A 78 1.54
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 ARG A 4 134.99 61.76
REMARK 500 1 PRO A 5 -169.16 -79.77
REMARK 500 1 LYS A 6 -74.96 -132.40
REMARK 500 1 THR A 11 -73.67 -99.40
REMARK 500 1 SER A 17 118.44 167.10
REMARK 500 1 PRO A 25 38.21 -82.83
REMARK 500 1 GLN A 26 27.75 36.44
REMARK 500 1 GLN A 28 92.40 41.24
REMARK 500 1 GLU A 40 -68.55 171.89
REMARK 500 1 ALA A 49 102.12 -41.94
REMARK 500 1 ASP A 51 -34.75 -130.22
REMARK 500 1 LEU A 62 -126.97 -106.19
REMARK 500 1 ARG A 63 -55.21 172.53
REMARK 500 1 HIS A 76 89.62 -177.49
REMARK 500 1 ASP A 77 -58.20 64.63
REMARK 500 1 ASP A 78 66.11 -174.46
REMARK 500 1 THR A 90 105.56 -59.95
REMARK 500 1 ALA A 91 102.29 -44.29
REMARK 500 2 ARG A 4 96.03 2.21
REMARK 500 2 SER A 17 108.82 176.74
REMARK 500 2 PRO A 25 -163.91 -73.89
REMARK 500 2 GLN A 28 105.05 54.35
REMARK 500 2 PRO A 39 36.06 -85.00
REMARK 500 2 GLU A 40 -72.59 -151.89
REMARK 500 2 PRO A 50 -164.07 -74.01
REMARK 500 2 GLU A 53 -32.00 -146.06
REMARK 500 2 SER A 66 135.71 -170.45
REMARK 500 2 HIS A 76 -155.17 -151.39
REMARK 500 2 ASP A 78 63.50 176.49
REMARK 500 2 MET A 79 -169.79 -125.95
REMARK 500 2 GLU A 80 61.26 -152.22
REMARK 500 2 GLN A 88 139.89 179.67
REMARK 500 2 ALA A 91 179.60 -52.36
REMARK 500 3 ARG A 4 119.36 63.40
REMARK 500 3 PRO A 5 -160.06 -72.51
REMARK 500 3 LYS A 6 144.66 -177.40
REMARK 500 3 THR A 11 -77.06 -96.47
REMARK 500 3 SER A 17 115.71 -172.54
REMARK 500 3 SER A 24 161.29 -42.63
REMARK 500 3 GLU A 40 -60.83 -164.12
REMARK 500 3 PRO A 50 -165.75 -74.17
REMARK 500 3 LEU A 62 -162.20 -114.32
REMARK 500 3 GLU A 67 85.84 -56.97
REMARK 500 3 HIS A 76 101.45 -177.73
REMARK 500 3 ASP A 77 -74.14 62.32
REMARK 500 3 ASP A 78 58.09 -158.74
REMARK 500 3 ALA A 91 -161.12 -61.47
REMARK 500 4 ILE A 2 -177.68 44.60
REMARK 500 4 ARG A 4 112.53 60.77
REMARK 500 4 LYS A 6 -59.43 -128.87
REMARK 500
REMARK 500 THIS ENTRY HAS 316 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 4 0.27 SIDE CHAIN
REMARK 500 1 ARG A 31 0.17 SIDE CHAIN
REMARK 500 1 ARG A 33 0.32 SIDE CHAIN
REMARK 500 1 ARG A 63 0.25 SIDE CHAIN
REMARK 500 2 ARG A 4 0.30 SIDE CHAIN
REMARK 500 2 ARG A 31 0.28 SIDE CHAIN
REMARK 500 2 ARG A 33 0.31 SIDE CHAIN
REMARK 500 2 ARG A 63 0.32 SIDE CHAIN
REMARK 500 3 ARG A 4 0.10 SIDE CHAIN
REMARK 500 3 ARG A 31 0.26 SIDE CHAIN
REMARK 500 3 ARG A 33 0.32 SIDE CHAIN
REMARK 500 3 ARG A 63 0.10 SIDE CHAIN
REMARK 500 4 ARG A 4 0.29 SIDE CHAIN
REMARK 500 4 ARG A 31 0.25 SIDE CHAIN
REMARK 500 4 ARG A 33 0.11 SIDE CHAIN
REMARK 500 4 ARG A 63 0.24 SIDE CHAIN
REMARK 500 5 ARG A 4 0.32 SIDE CHAIN
REMARK 500 5 ARG A 31 0.30 SIDE CHAIN
REMARK 500 5 ARG A 33 0.31 SIDE CHAIN
REMARK 500 5 ARG A 63 0.17 SIDE CHAIN
REMARK 500 6 ARG A 4 0.30 SIDE CHAIN
REMARK 500 6 ARG A 31 0.29 SIDE CHAIN
REMARK 500 6 ARG A 33 0.23 SIDE CHAIN
REMARK 500 6 ARG A 63 0.24 SIDE CHAIN
REMARK 500 7 ARG A 4 0.32 SIDE CHAIN
REMARK 500 7 ARG A 31 0.19 SIDE CHAIN
REMARK 500 7 ARG A 33 0.28 SIDE CHAIN
REMARK 500 7 ARG A 63 0.24 SIDE CHAIN
REMARK 500 8 ARG A 4 0.29 SIDE CHAIN
REMARK 500 8 ARG A 31 0.30 SIDE CHAIN
REMARK 500 8 ARG A 33 0.30 SIDE CHAIN
REMARK 500 8 ARG A 63 0.31 SIDE CHAIN
REMARK 500 9 ARG A 4 0.29 SIDE CHAIN
REMARK 500 9 ARG A 31 0.22 SIDE CHAIN
REMARK 500 9 ARG A 33 0.32 SIDE CHAIN
REMARK 500 9 ARG A 63 0.31 SIDE CHAIN
REMARK 500 10 ARG A 4 0.30 SIDE CHAIN
REMARK 500 10 ARG A 31 0.29 SIDE CHAIN
REMARK 500 10 ARG A 33 0.32 SIDE CHAIN
REMARK 500 10 ARG A 63 0.32 SIDE CHAIN
REMARK 500 11 ARG A 4 0.18 SIDE CHAIN
REMARK 500 11 ARG A 31 0.27 SIDE CHAIN
REMARK 500 11 ARG A 33 0.27 SIDE CHAIN
REMARK 500 11 ARG A 63 0.27 SIDE CHAIN
REMARK 500 12 ARG A 4 0.32 SIDE CHAIN
REMARK 500 12 ARG A 31 0.21 SIDE CHAIN
REMARK 500 12 ARG A 33 0.31 SIDE CHAIN
REMARK 500 12 ARG A 63 0.29 SIDE CHAIN
REMARK 500 13 ARG A 4 0.24 SIDE CHAIN
REMARK 500 13 ARG A 31 0.32 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 79 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5027 RELATED DB: BMRB
REMARK 900 THE CHEMICAL SHIFT TABLE OF FIBRONECTIN
DBREF 1J8K A 1 94 UNP P02751 FINC_HUMAN 1631 1724
SEQRES 1 A 94 ASN ILE ASP ARG PRO LYS GLY LEU ALA PHE THR ASP VAL
SEQRES 2 A 94 ASP VAL ASP SER ILE LYS ILE ALA TRP GLU SER PRO GLN
SEQRES 3 A 94 GLY GLN VAL SER ARG TYR ARG VAL THR TYR SER SER PRO
SEQRES 4 A 94 GLU ASP GLY ILE HIS GLU LEU PHE PRO ALA PRO ASP GLY
SEQRES 5 A 94 GLU GLU ASP THR ALA GLU LEU GLN GLY LEU ARG PRO GLY
SEQRES 6 A 94 SER GLU TYR THR VAL SER VAL VAL ALA LEU HIS ASP ASP
SEQRES 7 A 94 MET GLU SER GLN PRO LEU ILE GLY THR GLN SER THR ALA
SEQRES 8 A 94 ILE PRO ALA
SHEET 1 A 3 ALA A 9 ASP A 14 0
SHEET 2 A 3 SER A 17 ALA A 21 -1 N SER A 17 O ASP A 14
SHEET 3 A 3 THR A 56 LEU A 59 -1 N ALA A 57 O ILE A 20
SHEET 1 B 4 GLY A 42 LEU A 46 0
SHEET 2 B 4 TYR A 32 SER A 38 -1 O VAL A 34 N LEU A 46
SHEET 3 B 4 GLU A 67 ALA A 74 -1 O THR A 69 N SER A 37
SHEET 4 B 4 LEU A 84 SER A 89 -1 O LEU A 84 N VAL A 72
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